메뉴 건너뛰기




Volumn 632, Issue , 2017, Pages 142-157

Structure, function, and mechanism of proline utilization A (PutA)

Author keywords

Aldehyde dehydrogenase; Enzyme hysteresis; Flavin dependent reaction; Flavoprotein; Multifunctional enzymes; proline catabolism; Protein structure; Substrate channeling

Indexed keywords

ENZYME; PROLINE; PROLINE UTILIZATION A; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; FLAVINE ADENINE NUCLEOTIDE; FLAVOPROTEIN; MEMBRANE PROTEIN; PROLINE DEHYDROGENASE; PUTA PROTEIN, BACTERIA; PYRROLINE 5 CARBOXYLATE DEHYDROGENASE;

EID: 85025439517     PISSN: 00039861     EISSN: 10960384     Source Type: Journal    
DOI: 10.1016/j.abb.2017.07.005     Document Type: Review
Times cited : (62)

References (93)
  • 2
    • 0029933685 scopus 로고    scopus 로고
    • Association of hyperprolinaemia type I and heparin cofactor II deficiency with CATCH 22 syndrome: evidence for a contiguous gene syndrome locating the proline oxidase gene
    • Jaeken, J., Goemans, N., Fryns, J.P., Francois, I., de Zegher, F., Association of hyperprolinaemia type I and heparin cofactor II deficiency with CATCH 22 syndrome: evidence for a contiguous gene syndrome locating the proline oxidase gene. J. Inherit. Metab. Dis. 19:3 (1996), 275–277.
    • (1996) J. Inherit. Metab. Dis. , vol.19 , Issue.3 , pp. 275-277
    • Jaeken, J.1    Goemans, N.2    Fryns, J.P.3    Francois, I.4    de Zegher, F.5
  • 6
    • 53849120906 scopus 로고    scopus 로고
    • PRODH variants and risk for schizophrenia
    • Willis, A., Bender, H.U., Steel, G., Valle, D., PRODH variants and risk for schizophrenia. Amino Acids 35:4 (2008), 673–679.
    • (2008) Amino Acids , vol.35 , Issue.4 , pp. 673-679
    • Willis, A.1    Bender, H.U.2    Steel, G.3    Valle, D.4
  • 8
    • 85004092989 scopus 로고    scopus 로고
    • Cytosolic accumulation of L-proline disrupts GABA-ergic transmission through GAD blockade
    • Crabtree, G.W., Park, A.J., Gordon, J.A., Gogos, J.A., Cytosolic accumulation of L-proline disrupts GABA-ergic transmission through GAD blockade. Cell Rep. 17:2 (2016), 570–582.
    • (2016) Cell Rep. , vol.17 , Issue.2 , pp. 570-582
    • Crabtree, G.W.1    Park, A.J.2    Gordon, J.A.3    Gogos, J.A.4
  • 9
    • 84861891911 scopus 로고    scopus 로고
    • Reprogramming of proline and glutamine metabolism contributes to the proliferative and metabolic responses regulated by oncogenic transcription factor c-MYC
    • Liu, W., Le, A., Hancock, C., Lane, A.N., Dang, C.V., Fan, T.W., Phang, J.M., Reprogramming of proline and glutamine metabolism contributes to the proliferative and metabolic responses regulated by oncogenic transcription factor c-MYC. Proc. Natl. Acad. Sci. U. S. A. 109:23 (2012), 8983–8988.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , Issue.23 , pp. 8983-8988
    • Liu, W.1    Le, A.2    Hancock, C.3    Lane, A.N.4    Dang, C.V.5    Fan, T.W.6    Phang, J.M.7
  • 10
    • 84871240190 scopus 로고    scopus 로고
    • Proline dehydrogenase (oxidase) in cancer
    • Liu, W., Phang, J.M., Proline dehydrogenase (oxidase) in cancer. Biofactors 38:6 (2012), 398–406.
    • (2012) Biofactors , vol.38 , Issue.6 , pp. 398-406
    • Liu, W.1    Phang, J.M.2
  • 13
    • 77953541273 scopus 로고    scopus 로고
    • Purification and characterization of Put1p from Saccharomyces cerevisiae
    • Wanduragala, S., Sanyal, N., Liang, X., Becker, D.F., Purification and characterization of Put1p from Saccharomyces cerevisiae. Arch. Biochem. Biophys. 498:2 (2010), 136–142.
    • (2010) Arch. Biochem. Biophys. , vol.498 , Issue.2 , pp. 136-142
    • Wanduragala, S.1    Sanyal, N.2    Liang, X.3    Becker, D.F.4
  • 16
    • 0035266127 scopus 로고    scopus 로고
    • Proline oxidase, encoded by p53-induced gene-6, catalyzes the generation of proline-dependent reactive oxygen species
    • Donald, S.P., Sun, X.Y., Hu, C.A., Yu, J., Mei, J.M., Valle, D., Phang, J.M., Proline oxidase, encoded by p53-induced gene-6, catalyzes the generation of proline-dependent reactive oxygen species. Cancer Res. 61:5 (2001), 1810–1815.
    • (2001) Cancer Res. , vol.61 , Issue.5 , pp. 1810-1815
    • Donald, S.P.1    Sun, X.Y.2    Hu, C.A.3    Yu, J.4    Mei, J.M.5    Valle, D.6    Phang, J.M.7
  • 17
    • 84859475161 scopus 로고    scopus 로고
    • Impaired insulin/IGF1 signaling extends life span by promoting mitochondrial L-proline catabolism to induce a transient ROS signal
    • Zarse, K., Schmeisser, S., Groth, M., Priebe, S., Beuster, G., Kuhlow, D., Guthke, R., Platzer, M., Kahn, C.R., Ristow, M., Impaired insulin/IGF1 signaling extends life span by promoting mitochondrial L-proline catabolism to induce a transient ROS signal. Cell Metab. 15:4 (2012), 451–465.
    • (2012) Cell Metab. , vol.15 , Issue.4 , pp. 451-465
    • Zarse, K.1    Schmeisser, S.2    Groth, M.3    Priebe, S.4    Beuster, G.5    Kuhlow, D.6    Guthke, R.7    Platzer, M.8    Kahn, C.R.9    Ristow, M.10
  • 18
    • 75749084035 scopus 로고    scopus 로고
    • Proline: a multifunctional amino acid
    • Szabados, L., Savoure, A., Proline: a multifunctional amino acid. Trends Plant Sci. 15:2 (2010), 89–97.
    • (2010) Trends Plant Sci. , vol.15 , Issue.2 , pp. 89-97
    • Szabados, L.1    Savoure, A.2
  • 20
    • 84920840827 scopus 로고    scopus 로고
    • Proline metabolism increases katG expression and oxidative stress resistance in Escherichia coli
    • Zhang, L., Alfano, J.R., Becker, D.F., Proline metabolism increases katG expression and oxidative stress resistance in Escherichia coli. J. Bacteriol. 197:3 (2015), 431–440.
    • (2015) J. Bacteriol. , vol.197 , Issue.3 , pp. 431-440
    • Zhang, L.1    Alfano, J.R.2    Becker, D.F.3
  • 21
    • 53849128901 scopus 로고    scopus 로고
    • Structural biology of proline catabolism
    • Tanner, J.J., Structural biology of proline catabolism. Amino Acids 35:4 (2008), 719–730.
    • (2008) Amino Acids , vol.35 , Issue.4 , pp. 719-730
    • Tanner, J.J.1
  • 22
    • 41149157883 scopus 로고    scopus 로고
    • Possible involvement of put A gene in Helicobacter pylori colonization in the stomach and motility
    • Nakajima, K., Inatsu, S., Mizote, T., Nagata, Y., Aoyama, K., Fukuda, Y., Nagata, K., Possible involvement of put A gene in Helicobacter pylori colonization in the stomach and motility. Biomed. Res. 29:1 (2008), 9–18.
    • (2008) Biomed. Res. , vol.29 , Issue.1 , pp. 9-18
    • Nakajima, K.1    Inatsu, S.2    Mizote, T.3    Nagata, Y.4    Aoyama, K.5    Fukuda, Y.6    Nagata, K.7
  • 23
    • 46449111827 scopus 로고    scopus 로고
    • Characterization of a Helicobacter hepaticus putA mutant strain in host colonization and oxidative stress
    • Krishnan, N., Doster, A.R., Duhamel, G.E., Becker, D.F., Characterization of a Helicobacter hepaticus putA mutant strain in host colonization and oxidative stress. Infect. Immun. 76:7 (2008), 3037–3044.
    • (2008) Infect. Immun. , vol.76 , Issue.7 , pp. 3037-3044
    • Krishnan, N.1    Doster, A.R.2    Duhamel, G.E.3    Becker, D.F.4
  • 24
    • 84920913770 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis proliferation begins with NtrY/NtrX and PutA/GlnA upregulation and CtrA degradation induced by proline and glutamine uptake
    • 14
    • Cheng, Z., Lin, M., Rikihisa, Y., Ehrlichia chaffeensis proliferation begins with NtrY/NtrX and PutA/GlnA upregulation and CtrA degradation induced by proline and glutamine uptake. mBio, 5(6), 2014, e02141 14.
    • (2014) mBio , vol.5 , Issue.6 , pp. e02141
    • Cheng, Z.1    Lin, M.2    Rikihisa, Y.3
  • 25
    • 0042424963 scopus 로고    scopus 로고
    • L-Serine, D- and L-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels
    • Nagata, K., Nagata, Y., Sato, T., Fujino, M.A., Nakajima, K., Tamura, T., L-Serine, D- and L-proline and alanine as respiratory substrates of Helicobacter pylori: correlation between in vitro and in vivo amino acid levels. Microbiology 149:Pt 8 (2003), 2023–2030.
    • (2003) Microbiology , vol.149 , pp. 2023-2030
    • Nagata, K.1    Nagata, Y.2    Sato, T.3    Fujino, M.A.4    Nakajima, K.5    Tamura, T.6
  • 26
    • 84860314428 scopus 로고    scopus 로고
    • Unique structural features and sequence motifs of proline utilization A (PutA)
    • Singh, R.K., Tanner, J.J., Unique structural features and sequence motifs of proline utilization A (PutA). Front. Biosci. (Landmark Ed.) 17 (2012), 556–568.
    • (2012) Front. Biosci. (Landmark Ed.) , vol.17 , pp. 556-568
    • Singh, R.K.1    Tanner, J.J.2
  • 27
    • 84857706529 scopus 로고    scopus 로고
    • Substrate channeling in proline metabolism
    • Arentson, B.W., Sanyal, N., Becker, D.F., Substrate channeling in proline metabolism. Front. Biosci. 17 (2012), 375–388.
    • (2012) Front. Biosci. , vol.17 , pp. 375-388
    • Arentson, B.W.1    Sanyal, N.2    Becker, D.F.3
  • 28
    • 79951871588 scopus 로고    scopus 로고
    • Flavin redox switching of protein functions
    • Becker, D.F., Zhu, W., Moxley, M.A., Flavin redox switching of protein functions. Antioxid. Redox Signal. 14:6 (2011), 1079–1091.
    • (2011) Antioxid. Redox Signal. , vol.14 , Issue.6 , pp. 1079-1091
    • Becker, D.F.1    Zhu, W.2    Moxley, M.A.3
  • 29
    • 85020737804 scopus 로고    scopus 로고
    • Structure and characterization of a class 3B proline utilization A: ligand-induced dimerization and importance of the C-terminal domain for catalysis
    • Korasick, D., Gamage, T.T., Christgen, S., Stiers, K.M., Beamer, L.J., Henzl, M.T., Becker, D.F., Tanner, J.J., Structure and characterization of a class 3B proline utilization A: ligand-induced dimerization and importance of the C-terminal domain for catalysis. J. Biol. Chem. 292:23 (2017 Jun 9), 9652–9665, 10.1074/jbc.M117.786855.
    • (2017) J. Biol. Chem. , vol.292 , Issue.23 , pp. 9652-9665
    • Korasick, D.1    Gamage, T.T.2    Christgen, S.3    Stiers, K.M.4    Beamer, L.J.5    Henzl, M.T.6    Becker, D.F.7    Tanner, J.J.8
  • 30
    • 84995427088 scopus 로고    scopus 로고
    • Structures of proline utilization A (PutA) reveal the fold and functions of the aldehyde dehydrogenase superfamily domain of unknown function
    • Luo, M., Gamage, T.T., Arentson, B.W., Schlasner, K.N., Becker, D.F., Tanner, J.J., Structures of proline utilization A (PutA) reveal the fold and functions of the aldehyde dehydrogenase superfamily domain of unknown function. J. Biol. Chem. 291:46 (2016), 24065–24075.
    • (2016) J. Biol. Chem. , vol.291 , Issue.46 , pp. 24065-24075
    • Luo, M.1    Gamage, T.T.2    Arentson, B.W.3    Schlasner, K.N.4    Becker, D.F.5    Tanner, J.J.6
  • 32
    • 84895795810 scopus 로고    scopus 로고
    • Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site
    • Singh, H., Arentson, B.W., Becker, D.F., Tanner, J.J., Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site. Proc. Nat. Acad. Sci. U. S. A. 111:9 (2014), 3389–3394.
    • (2014) Proc. Nat. Acad. Sci. U. S. A. , vol.111 , Issue.9 , pp. 3389-3394
    • Singh, H.1    Arentson, B.W.2    Becker, D.F.3    Tanner, J.J.4
  • 33
    • 85026516346 scopus 로고    scopus 로고
    • Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure
    • Korasick, D.A., Singh, H., Pemberton, T.A., Luo, M., Dhatwalia, R., Tanner, J.J., Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J., 2017, 10.1111/febs.14165.
    • (2017) FEBS J.
    • Korasick, D.A.1    Singh, H.2    Pemberton, T.A.3    Luo, M.4    Dhatwalia, R.5    Tanner, J.J.6
  • 34
    • 84871285122 scopus 로고    scopus 로고
    • Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release
    • Luo, M., Arentson, B.W., Srivastava, D., Becker, D.F., Tanner, J.J., Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release. Biochemistry 51:50 (2012), 10099–10108.
    • (2012) Biochemistry , vol.51 , Issue.50 , pp. 10099-10108
    • Luo, M.1    Arentson, B.W.2    Srivastava, D.3    Becker, D.F.4    Tanner, J.J.5
  • 35
    • 84905980079 scopus 로고    scopus 로고
    • Kinetic and structural characterization of tunnel-perturbing mutants in Bradyrhizobium japonicum proline utilization A
    • Arentson, B.W., Luo, M., Pemberton, T.A., Tanner, J.J., Becker, D.F., Kinetic and structural characterization of tunnel-perturbing mutants in Bradyrhizobium japonicum proline utilization A. Biochemistry 53:31 (2014), 5150–5161.
    • (2014) Biochemistry , vol.53 , Issue.31 , pp. 5150-5161
    • Arentson, B.W.1    Luo, M.2    Pemberton, T.A.3    Tanner, J.J.4    Becker, D.F.5
  • 36
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E., Henrick, K., Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D. Biol. Crystallogr. 60:Pt 12 Pt 1 (2004), 2256–2268.
    • (2004) Acta Crystallogr. D. Biol. Crystallogr. , vol.60 , Issue.Pt 12 Pt 1 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 37
    • 84907487629 scopus 로고    scopus 로고
    • Evidence that the C-Terminal domain of a type B PutA protein contributes to aldehyde dehydrogenase activity and substrate channeling
    • Luo, M., Christgen, S., Sanyal, N., Arentson, B.W., Becker, D.F., Tanner, J.J., Evidence that the C-Terminal domain of a type B PutA protein contributes to aldehyde dehydrogenase activity and substrate channeling. Biochemistry 53:35 (2014), 5661–5673.
    • (2014) Biochemistry , vol.53 , Issue.35 , pp. 5661-5673
    • Luo, M.1    Christgen, S.2    Sanyal, N.3    Arentson, B.W.4    Becker, D.F.5    Tanner, J.J.6
  • 38
    • 23944437104 scopus 로고    scopus 로고
    • Morpheeins–a new structural paradigm for allosteric regulation
    • Jaffe, E.K., Morpheeins–a new structural paradigm for allosteric regulation. Trends Biochem. Sci. 30:9 (2005), 490–497.
    • (2005) Trends Biochem. Sci. , vol.30 , Issue.9 , pp. 490-497
    • Jaffe, E.K.1
  • 39
    • 84857865522 scopus 로고    scopus 로고
    • Dynamic dissociating homo-oligomers and the control of protein function
    • Selwood, T., Jaffe, E.K., Dynamic dissociating homo-oligomers and the control of protein function. Arch. Biochem. Biophys. 519:2 (2012), 131–143.
    • (2012) Arch. Biochem. Biophys. , vol.519 , Issue.2 , pp. 131-143
    • Selwood, T.1    Jaffe, E.K.2
  • 40
    • 33751088044 scopus 로고    scopus 로고
    • Crystal structures of the DNA-binding domain of Escherichia coli proline utilization A flavoprotein and analysis of the role of Lys9 in DNA recognition
    • Larson, J.D., Jenkins, J.L., Schuermann, J.P., Zhou, Y., Becker, D.F., Tanner, J.J., Crystal structures of the DNA-binding domain of Escherichia coli proline utilization A flavoprotein and analysis of the role of Lys9 in DNA recognition. Protein Sci. 15 (2006), 1–12.
    • (2006) Protein Sci. , vol.15 , pp. 1-12
    • Larson, J.D.1    Jenkins, J.L.2    Schuermann, J.P.3    Zhou, Y.4    Becker, D.F.5    Tanner, J.J.6
  • 42
    • 83355169696 scopus 로고    scopus 로고
    • Small-angle X-ray scattering studies of the oligomeric state and quaternary structure of the trifunctional proline utilization A (PutA) flavoprotein from Escherichia coli
    • Singh, R.K., Larson, J.D., Zhu, W., Rambo, R.P., Hura, G.L., Becker, D.F., Tanner, J.J., Small-angle X-ray scattering studies of the oligomeric state and quaternary structure of the trifunctional proline utilization A (PutA) flavoprotein from Escherichia coli. J. Biol. Chem. 286:50 (2011), 43144–43153.
    • (2011) J. Biol. Chem. , vol.286 , Issue.50 , pp. 43144-43153
    • Singh, R.K.1    Larson, J.D.2    Zhu, W.3    Rambo, R.P.4    Hura, G.L.5    Becker, D.F.6    Tanner, J.J.7
  • 43
    • 0037312937 scopus 로고    scopus 로고
    • Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
    • Lee, Y.H., Nadaraia, S., Gu, D., Becker, D.F., Tanner, J.J., Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein. Nat. Struct. Biol. 10:2 (2003), 109–114.
    • (2003) Nat. Struct. Biol. , vol.10 , Issue.2 , pp. 109-114
    • Lee, Y.H.1    Nadaraia, S.2    Gu, D.3    Becker, D.F.4    Tanner, J.J.5
  • 44
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold, K., Bordoli, L., Kopp, J., Schwede, T., The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22:2 (2006), 195–201.
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 45
    • 81755173365 scopus 로고    scopus 로고
    • Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli
    • Moxley, M.A., Tanner, J.J., Becker, D.F., Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli. Arch. Biochem. Biophys. 516:2 (2011), 113–120.
    • (2011) Arch. Biochem. Biophys. , vol.516 , Issue.2 , pp. 113-120
    • Moxley, M.A.1    Tanner, J.J.2    Becker, D.F.3
  • 46
    • 84856946727 scopus 로고    scopus 로고
    • Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein
    • Moxley, M.A., Becker, D.F., Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein. Biochemistry 51:1 (2012), 511–520.
    • (2012) Biochemistry , vol.51 , Issue.1 , pp. 511-520
    • Moxley, M.A.1    Becker, D.F.2
  • 47
    • 0019805440 scopus 로고
    • Enzymatic properties of the purified putA protein from Salmonella typhimurium
    • Menzel, R., Roth, J., Enzymatic properties of the purified putA protein from Salmonella typhimurium. J. Biol. Chem. 256:18 (1981), 9762–9766.
    • (1981) J. Biol. Chem. , vol.256 , Issue.18 , pp. 9762-9766
    • Menzel, R.1    Roth, J.2
  • 48
    • 0037881834 scopus 로고    scopus 로고
    • Flavin redox state triggers conformational changes in the PutA protein from Escherichia coli
    • Zhu, W., Becker, D.F., Flavin redox state triggers conformational changes in the PutA protein from Escherichia coli. Biochemistry 42:18 (2003), 5469–5477.
    • (2003) Biochemistry , vol.42 , Issue.18 , pp. 5469-5477
    • Zhu, W.1    Becker, D.F.2
  • 49
    • 84883511429 scopus 로고    scopus 로고
    • Structural basis of substrate selectivity of Delta(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): semialdehyde chain length
    • Pemberton, T.A., Tanner, J.J., Structural basis of substrate selectivity of Delta(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): semialdehyde chain length. Arch. Biochem. Biophys. 538:1 (2013), 34–40.
    • (2013) Arch. Biochem. Biophys. , vol.538 , Issue.1 , pp. 34-40
    • Pemberton, T.A.1    Tanner, J.J.2
  • 50
    • 0036707995 scopus 로고    scopus 로고
    • A structurally conserved water molecule in Rossmann dinucleotide-binding domains
    • Bottoms, C.A., Smith, P.E., Tanner, J.J., A structurally conserved water molecule in Rossmann dinucleotide-binding domains. Protein Sci. 11:9 (2002), 2125–2137.
    • (2002) Protein Sci. , vol.11 , Issue.9 , pp. 2125-2137
    • Bottoms, C.A.1    Smith, P.E.2    Tanner, J.J.3
  • 51
    • 85018246845 scopus 로고    scopus 로고
    • Resolving the cofactor binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1
    • Christensen, E.M., Patel, S.M., Korasick, D.A., Campbell, A.C., Krause, K.L., Becker, D.F., Tanner, J.J., Resolving the cofactor binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1. J. Biol. Chem. 292:17 (2017 Apr 28), 7233–7243, 10.1074/jbc.M117.780288.
    • (2017) J. Biol. Chem. , vol.292 , Issue.17 , pp. 7233-7243
    • Christensen, E.M.1    Patel, S.M.2    Korasick, D.A.3    Campbell, A.C.4    Krause, K.L.5    Becker, D.F.6    Tanner, J.J.7
  • 52
    • 84893659587 scopus 로고    scopus 로고
    • Evidence for hysteretic substrate channeling in the proline dehydrogenase and delta1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA)
    • Moxley, M.A., Sanyal, N., Krishnan, N., Tanner, J.J., Becker, D.F., Evidence for hysteretic substrate channeling in the proline dehydrogenase and delta1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA). J. Biol. Chem. 289:6 (2014), 3639–3651.
    • (2014) J. Biol. Chem. , vol.289 , Issue.6 , pp. 3639-3651
    • Moxley, M.A.1    Sanyal, N.2    Krishnan, N.3    Tanner, J.J.4    Becker, D.F.5
  • 53
    • 0032872139 scopus 로고    scopus 로고
    • Fundamental mechanisms of substrate channeling
    • Anderson, K.S., Fundamental mechanisms of substrate channeling. Methods Enzymol. 308 (1999), 111–145.
    • (1999) Methods Enzymol. , vol.308 , pp. 111-145
    • Anderson, K.S.1
  • 54
    • 1842610703 scopus 로고    scopus 로고
    • Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate
    • van den Heuvel, R.H., Curti, B., Vanoni, M.A., Mattevi, A., Glutamate synthase: a fascinating pathway from L-glutamine to L-glutamate. Cell Mol. Life Sci. 61:6 (2004), 669–681.
    • (2004) Cell Mol. Life Sci. , vol.61 , Issue.6 , pp. 669-681
    • van den Heuvel, R.H.1    Curti, B.2    Vanoni, M.A.3    Mattevi, A.4
  • 55
    • 0041465718 scopus 로고    scopus 로고
    • Channelling and formation of ‘active’ formaldehyde in dimethylglycine oxidase
    • Leys, D., Basran, J., Scrutton, N.S., Channelling and formation of ‘active’ formaldehyde in dimethylglycine oxidase. EMBO J. 22:16 (2003), 4038–4048.
    • (2003) EMBO J. , vol.22 , Issue.16 , pp. 4038-4048
    • Leys, D.1    Basran, J.2    Scrutton, N.S.3
  • 56
    • 67650533781 scopus 로고    scopus 로고
    • An internal reaction chamber in dimethylglycine oxidase provides efficient protection from exposure to toxic formaldehyde
    • Tralau, T., Lafite, P., Levy, C., Combe, J.P., Scrutton, N.S., Leys, D., An internal reaction chamber in dimethylglycine oxidase provides efficient protection from exposure to toxic formaldehyde. J. Biol. Chem. 284:26 (2009), 17826–17834.
    • (2009) J. Biol. Chem. , vol.284 , Issue.26 , pp. 17826-17834
    • Tralau, T.1    Lafite, P.2    Levy, C.3    Combe, J.P.4    Scrutton, N.S.5    Leys, D.6
  • 58
    • 77953810360 scopus 로고    scopus 로고
    • Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes
    • Herguedas, B., Martinez-Julvez, M., Frago, S., Medina, M., Hermoso, J.A., Oligomeric state in the crystal structure of modular FAD synthetase provides insights into its sequential catalysis in prokaryotes. J. Mol. Biol. 400:2 (2010), 218–230.
    • (2010) J. Mol. Biol. , vol.400 , Issue.2 , pp. 218-230
    • Herguedas, B.1    Martinez-Julvez, M.2    Frago, S.3    Medina, M.4    Hermoso, J.A.5
  • 59
    • 84921445381 scopus 로고    scopus 로고
    • First evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactions
    • Sanyal, N., Arentson, B.W., Luo, M., Tanner, J.J., Becker, D.F., First evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactions. J. Biol. Chem. 290:4 (2015), 2225–2234.
    • (2015) J. Biol. Chem. , vol.290 , Issue.4 , pp. 2225-2234
    • Sanyal, N.1    Arentson, B.W.2    Luo, M.3    Tanner, J.J.4    Becker, D.F.5
  • 60
    • 0033617187 scopus 로고    scopus 로고
    • The molecular basis of substrate channeling
    • Miles, E.W., Rhee, S.G., Davies, D.R., The molecular basis of substrate channeling. J. Biol. Chem. 274:18 (1999), 12193–12196.
    • (1999) J. Biol. Chem. , vol.274 , Issue.18 , pp. 12193-12196
    • Miles, E.W.1    Rhee, S.G.2    Davies, D.R.3
  • 62
    • 84999036827 scopus 로고    scopus 로고
    • Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA
    • Arentson, B.W., Hayes, E.L., Zhu, W., Singh, H., Tanner, J.J., Becker, D.F., Engineering a trifunctional proline utilization A chimaera by fusing a DNA-binding domain to a bifunctional PutA. Biosci. Rep., 36(6), 2016, e00413.
    • (2016) Biosci. Rep. , vol.36 , Issue.6 , pp. e00413
    • Arentson, B.W.1    Hayes, E.L.2    Zhu, W.3    Singh, H.4    Tanner, J.J.5    Becker, D.F.6
  • 63
    • 74949118627 scopus 로고    scopus 로고
    • The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction
    • Srivastava, D., Zhu, W., Johnson, W.H. Jr., Whitman, C.P., Becker, D.F., Tanner, J.J., The structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction. Biochemistry 49:3 (2010), 560–569.
    • (2010) Biochemistry , vol.49 , Issue.3 , pp. 560-569
    • Srivastava, D.1    Zhu, W.2    Johnson, W.H.3    Whitman, C.P.4    Becker, D.F.5    Tanner, J.J.6
  • 64
    • 0018401599 scopus 로고
    • Slow transitions and hysteretic behavior in enzymes
    • Frieden, C., Slow transitions and hysteretic behavior in enzymes. Annu. Rev. Biochem. 48 (1979), 471–489.
    • (1979) Annu. Rev. Biochem. , vol.48 , pp. 471-489
    • Frieden, C.1
  • 65
    • 84865785874 scopus 로고    scopus 로고
    • Functional roles of slow enzyme conformational changes in network dynamics
    • Wu, Z., Xing, J., Functional roles of slow enzyme conformational changes in network dynamics. Biophys. J. 103:5 (2012), 1052–1059.
    • (2012) Biophys. J. , vol.103 , Issue.5 , pp. 1052-1059
    • Wu, Z.1    Xing, J.2
  • 66
    • 33846185960 scopus 로고    scopus 로고
    • Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2’-OH group in regulating PutA-membrane binding
    • Zhang, W., Zhang, M., Zhu, W., Zhou, Y., Wanduragala, S., Rewinkel, D., Tanner, J.J., Becker, D.F., Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2’-OH group in regulating PutA-membrane binding. Biochemistry 46:2 (2007), 483–491.
    • (2007) Biochemistry , vol.46 , Issue.2 , pp. 483-491
    • Zhang, W.1    Zhang, M.2    Zhu, W.3    Zhou, Y.4    Wanduragala, S.5    Rewinkel, D.6    Tanner, J.J.7    Becker, D.F.8
  • 69
    • 0025006579 scopus 로고
    • The tryptophan synthase bienzyme complex transfers indole between the alpha- and beta-sites via a 25-30 A long tunnel
    • Dunn, M.F., Aguilar, V., Brzović P., Drewe, W.F., Houben, K.F., Leja, C.A., Roy, M., The tryptophan synthase bienzyme complex transfers indole between the alpha- and beta-sites via a 25-30 A long tunnel. Biochemistry 29:37 (1990), 8598–8607.
    • (1990) Biochemistry , vol.29 , Issue.37 , pp. 8598-8607
    • Dunn, M.F.1    Aguilar, V.2    Brzović, P.3    Drewe, W.F.4    Houben, K.F.5    Leja, C.A.6    Roy, M.7
  • 70
    • 0016835064 scopus 로고
    • Influence of an aggregated multienzyme system on transient time: kinetic evidence for compartmentation by an aromatic-amino-acid synthesizing complex of Neurospora crassa
    • Welch, G.R., Gaertner, F.H., Influence of an aggregated multienzyme system on transient time: kinetic evidence for compartmentation by an aromatic-amino-acid synthesizing complex of Neurospora crassa. Proc. Natl. Acad. Sci. U. S. A. 72:11 (1975), 4218–4222.
    • (1975) Proc. Natl. Acad. Sci. U. S. A. , vol.72 , Issue.11 , pp. 4218-4222
    • Welch, G.R.1    Gaertner, F.H.2
  • 71
    • 0031406496 scopus 로고    scopus 로고
    • Electrostatic channeling of substrates between enzyme active sites: comparison of simulation and experiment
    • Elcock, A.H., Huber, G.A., McCammon, J.A., Electrostatic channeling of substrates between enzyme active sites: comparison of simulation and experiment. Biochemistry 36:51 (1997), 16049–16058.
    • (1997) Biochemistry , vol.36 , Issue.51 , pp. 16049-16058
    • Elcock, A.H.1    Huber, G.A.2    McCammon, J.A.3
  • 72
    • 0019321917 scopus 로고
    • The overall synthesis of L-5,6-dihydroorotate by multienzymatic protein pyr1-3 from hamster cells. Kinetic studies, substrate channeling, and the effects of inhibitors
    • Christopherson, R.I., Jones, M.E., The overall synthesis of L-5,6-dihydroorotate by multienzymatic protein pyr1-3 from hamster cells. Kinetic studies, substrate channeling, and the effects of inhibitors. J. Biol. Chem. 255:23 (1980), 11381–11395.
    • (1980) J. Biol. Chem. , vol.255 , Issue.23 , pp. 11381-11395
    • Christopherson, R.I.1    Jones, M.E.2
  • 73
    • 68749106118 scopus 로고    scopus 로고
    • New roles of flavoproteins in molecular cell biology: an unexpected role for quinone reductases as regulators of proteasomal degradation
    • Sollner, S., Macheroux, P., New roles of flavoproteins in molecular cell biology: an unexpected role for quinone reductases as regulators of proteasomal degradation. FEBS J. 276:16 (2009), 4313–4324.
    • (2009) FEBS J. , vol.276 , Issue.16 , pp. 4313-4324
    • Sollner, S.1    Macheroux, P.2
  • 74
    • 4544232470 scopus 로고    scopus 로고
    • Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities
    • Liger, D., Graille, M., Zhou, C.Z., Leulliot, N., Quevillon-Cheruel, S., Blondeau, K., Janin, J., van Tilbeurgh, H., Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities. J. Biol. Chem. 279:33 (2004), 34890–34897.
    • (2004) J. Biol. Chem. , vol.279 , Issue.33 , pp. 34890-34897
    • Liger, D.1    Graille, M.2    Zhou, C.Z.3    Leulliot, N.4    Quevillon-Cheruel, S.5    Blondeau, K.6    Janin, J.7    van Tilbeurgh, H.8
  • 75
    • 70149114201 scopus 로고    scopus 로고
    • Mechanism of flavin reduction and oxidation in the redox-sensing quinone reductase Lot6p from Saccharomyces cerevisiae
    • Sollner, S., Deller, S., Macheroux, P., Palfey, B.A., Mechanism of flavin reduction and oxidation in the redox-sensing quinone reductase Lot6p from Saccharomyces cerevisiae. Biochemistry 48:36 (2009), 8636–8643.
    • (2009) Biochemistry , vol.48 , Issue.36 , pp. 8636-8643
    • Sollner, S.1    Deller, S.2    Macheroux, P.3    Palfey, B.A.4
  • 76
    • 84876513000 scopus 로고    scopus 로고
    • Chloroquine binding reveals flavin redox switch function of quinone reductase 2
    • Leung, K.K., Shilton, B.H., Chloroquine binding reveals flavin redox switch function of quinone reductase 2. J. Biol. Chem. 288:16 (2013), 11242–11251.
    • (2013) J. Biol. Chem. , vol.288 , Issue.16 , pp. 11242-11251
    • Leung, K.K.1    Shilton, B.H.2
  • 77
    • 0035969989 scopus 로고    scopus 로고
    • Regulation of p53 stability and p53-dependent apoptosis by NADH quinone oxidoreductase 1
    • Asher, G., Lotem, J., Cohen, B., Sachs, L., Shaul, Y., Regulation of p53 stability and p53-dependent apoptosis by NADH quinone oxidoreductase 1. Proc. Natl. Acad. Sci. U. S. A. 98:3 (2001), 1188–1193.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , Issue.3 , pp. 1188-1193
    • Asher, G.1    Lotem, J.2    Cohen, B.3    Sachs, L.4    Shaul, Y.5
  • 78
    • 0024046723 scopus 로고
    • Regulation of proline utilization in Salmonella typhimurium: molecular characterization of the put operon, and DNA sequence of the put control region
    • Hahn, D.R., Myers, R.S., Kent, C.R., Maloy, S.R., Regulation of proline utilization in Salmonella typhimurium: molecular characterization of the put operon, and DNA sequence of the put control region. Mol. General Genet. MGG 213:1 (1988), 125–133.
    • (1988) Mol. General Genet. MGG , vol.213 , Issue.1 , pp. 125-133
    • Hahn, D.R.1    Myers, R.S.2    Kent, C.R.3    Maloy, S.R.4
  • 79
    • 0024116709 scopus 로고
    • Mapping of the multiple regulatory sites for putP and putA expression in the putC region of Escherichia coli
    • Nakao, T., Yamato, I., Anraku, Y., Mapping of the multiple regulatory sites for putP and putA expression in the putC region of Escherichia coli. Mol. General Genet. MGG 214:3 (1988), 379–388.
    • (1988) Mol. General Genet. MGG , vol.214 , Issue.3 , pp. 379-388
    • Nakao, T.1    Yamato, I.2    Anraku, Y.3
  • 80
    • 0026086022 scopus 로고
    • Regulation of proline utilization in enteric bacteria: cloning and characterization of the Klebsiella put control region
    • Chen, L.M., Maloy, S., Regulation of proline utilization in enteric bacteria: cloning and characterization of the Klebsiella put control region. J. Bacteriol. 173:2 (1991), 783–790.
    • (1991) J. Bacteriol. , vol.173 , Issue.2 , pp. 783-790
    • Chen, L.M.1    Maloy, S.2
  • 81
    • 0033591426 scopus 로고    scopus 로고
    • An Lrp-type transcriptional regulator from Agrobacterium tumefaciens condenses more than 100 nucleotides of DNA into globular nucleoprotein complexes
    • Jafri, S., Evoy, S., Cho, K., Craighead, H.G., Winans, S.C., An Lrp-type transcriptional regulator from Agrobacterium tumefaciens condenses more than 100 nucleotides of DNA into globular nucleoprotein complexes. J. Mol. Biol. 288:5 (1999), 811–824.
    • (1999) J. Mol. Biol. , vol.288 , Issue.5 , pp. 811-824
    • Jafri, S.1    Evoy, S.2    Cho, K.3    Craighead, H.G.4    Winans, S.C.5
  • 82
    • 24944562717 scopus 로고    scopus 로고
    • Exploring the proline-dependent conformational change in the multifunctional PutA flavoprotein by tryptophan fluorescence spectroscopy
    • Zhu, W., Becker, D.F., Exploring the proline-dependent conformational change in the multifunctional PutA flavoprotein by tryptophan fluorescence spectroscopy. Biochemistry 44:37 (2005), 12297–12306.
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12297-12306
    • Zhu, W.1    Becker, D.F.2
  • 83
    • 0030976040 scopus 로고    scopus 로고
    • Regulation of gene expression by repressor localization: biochemical evidence that membrane and DNA binding by the PutA protein are mutually exclusive
    • Muro-Pastor, A.M., Ostrovsky, P., Maloy, S., Regulation of gene expression by repressor localization: biochemical evidence that membrane and DNA binding by the PutA protein are mutually exclusive. J. Bacteriol. 179:8 (1997), 2788–2791.
    • (1997) J. Bacteriol. , vol.179 , Issue.8 , pp. 2788-2791
    • Muro-Pastor, A.M.1    Ostrovsky, P.2    Maloy, S.3
  • 84
    • 53849098986 scopus 로고    scopus 로고
    • Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli
    • Zhou, Y., Zhu, W., Bellur, P.S., Rewinkel, D., Becker, D.F., Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli. Amino Acids 35:4 (2008), 711–718.
    • (2008) Amino Acids , vol.35 , Issue.4 , pp. 711-718
    • Zhou, Y.1    Zhu, W.2    Bellur, P.S.3    Rewinkel, D.4    Becker, D.F.5
  • 85
    • 84880167030 scopus 로고    scopus 로고
    • Involvement of the beta3-alpha3 loop of the proline dehydrogenase domain in allosteric regulation of membrane association of proline utilization A
    • Zhu, W., Haile, A.M., Singh, R.K., Larson, J.D., Smithen, D., Chan, J.Y., Tanner, J.J., Becker, D.F., Involvement of the beta3-alpha3 loop of the proline dehydrogenase domain in allosteric regulation of membrane association of proline utilization A. Biochemistry 52:26 (2013), 4482–4491.
    • (2013) Biochemistry , vol.52 , Issue.26 , pp. 4482-4491
    • Zhu, W.1    Haile, A.M.2    Singh, R.K.3    Larson, J.D.4    Smithen, D.5    Chan, J.Y.6    Tanner, J.J.7    Becker, D.F.8
  • 86
    • 29244452111 scopus 로고    scopus 로고
    • Kinetic and thermodynamic analysis of Bradyrhizobium japonicum PutA-membrane associations
    • Zhang, W., Krishnan, N., Becker, D.F., Kinetic and thermodynamic analysis of Bradyrhizobium japonicum PutA-membrane associations. Archives Biochem. Biophys. 445:1 (2006), 174–183.
    • (2006) Archives Biochem. Biophys. , vol.445 , Issue.1 , pp. 174-183
    • Zhang, W.1    Krishnan, N.2    Becker, D.F.3
  • 87
    • 0019777101 scopus 로고
    • Purification of the putA gene product. A bifunctional membrane-bound protein from Salmonella typhimurium responsible for the two-step oxidation of proline to glutamate
    • Menzel, R., Roth, J., Purification of the putA gene product. A bifunctional membrane-bound protein from Salmonella typhimurium responsible for the two-step oxidation of proline to glutamate. J. Biol. Chem. 256:18 (1981), 9755–9761.
    • (1981) J. Biol. Chem. , vol.256 , Issue.18 , pp. 9755-9761
    • Menzel, R.1    Roth, J.2
  • 88
    • 0035900664 scopus 로고    scopus 로고
    • Spectroscopic and kinetic characterization of the bifunctional chorismate synthase from Neurospora crassa: evidence for a common binding site for 5-enolpyruvylshikimate 3-phosphate and NADPH
    • Kitzing, K., Macheroux, P., Amrhein, N., Spectroscopic and kinetic characterization of the bifunctional chorismate synthase from Neurospora crassa: evidence for a common binding site for 5-enolpyruvylshikimate 3-phosphate and NADPH. J. Biol. Chem. 276:46 (2001), 42658–42666.
    • (2001) J. Biol. Chem. , vol.276 , Issue.46 , pp. 42658-42666
    • Kitzing, K.1    Macheroux, P.2    Amrhein, N.3
  • 90
    • 0034482639 scopus 로고    scopus 로고
    • Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthase
    • Binda, C., Bossi, R.T., Wakatsuki, S., Arzt, S., Coda, A., Curti, B., Vanoni, M.A., Mattevi, A., Cross-talk and ammonia channeling between active centers in the unexpected domain arrangement of glutamate synthase. Struct. (Lond. Engl. 1993) 8:12 (2000), 1299–1308.
    • (2000) Struct. (Lond. Engl. 1993) , vol.8 , Issue.12 , pp. 1299-1308
    • Binda, C.1    Bossi, R.T.2    Wakatsuki, S.3    Arzt, S.4    Coda, A.5    Curti, B.6    Vanoni, M.A.7    Mattevi, A.8
  • 93
    • 84925374065 scopus 로고    scopus 로고
    • Diethylaminobenzaldehyde is a covalent, irreversible inactivator of ALDH7A1
    • Luo, M., Gates, K.S., Henzl, M.T., Tanner, J.J., Diethylaminobenzaldehyde is a covalent, irreversible inactivator of ALDH7A1. ACS Chem. Biol. 10:3 (2015), 693–697.
    • (2015) ACS Chem. Biol. , vol.10 , Issue.3 , pp. 693-697
    • Luo, M.1    Gates, K.S.2    Henzl, M.T.3    Tanner, J.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.