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Volumn 191, Issue 1-3, 2011, Pages 129-136

Enzymatic properties of ALDH1L2, a mitochondrial 10-formyltetrahydrofolate dehydrogenase

Author keywords

10 Formyltetrahydrofolate dehydrogenase; Aldehyde dehydrogenase; ALDH1L2; Folate metabolism; Mitochondria; Phosphopantetheinylation

Indexed keywords

COENZYME A; FORMYLTETRAHYDROFOLATE DEHYDROGENASE; OXIDOREDUCTASE; RECOMBINANT ENZYME; SERINE; UNCLASSIFIED DRUG;

EID: 79957575346     PISSN: 00092797     EISSN: 18727786     Source Type: Journal    
DOI: 10.1016/j.cbi.2011.01.008     Document Type: Conference Paper
Times cited : (39)

References (43)
  • 1
    • 0002942853 scopus 로고
    • Biochemical role of folate in cellular metabolism
    • L.B. Bailey (Ed.), Marcel Dekker, Inc., New York
    • C. Wagner, Biochemical role of folate in cellular metabolism, in: L.B. Bailey (Ed.), Folate in Health and Disease, Marcel Dekker, Inc., New York, 1995, pp. 23-42.
    • (1995) Folate in Health and Disease , pp. 23-42
    • Wagner, C.1
  • 2
    • 0001303908 scopus 로고
    • Experimental nutritional folate deficiency in man
    • V. Herbert, Experimental nutritional folate deficiency in man, Trans. Assoc. Am. Physicians 75 (1962) 307-320.
    • (1962) Trans. Assoc. Am. Physicians , vol.75 , pp. 307-320
    • Herbert, V.1
  • 4
    • 70350135470 scopus 로고    scopus 로고
    • Folic acid fortification: A double-edged sword
    • M. Lucock, Z. Yates, Folic acid fortification: a double-edged sword, Curr. Opin. Clin. Nutr. Metab. Care 12 (6) (2009) 555-564.
    • (2009) Curr. Opin. Clin. Nutr. Metab. Care , vol.12 , Issue.6 , pp. 555-564
    • Lucock, M.1    Yates, Z.2
  • 5
    • 51849127760 scopus 로고    scopus 로고
    • Folate-mediated one-carbon metabolism
    • J.T. Fox, P.J. Stover, Folate-mediated one-carbon metabolism, Vitam. Horm. 79 (2008) 1-44.
    • (2008) Vitam. Horm. , vol.79 , pp. 1-44
    • Fox, J.T.1    Stover, P.J.2
  • 6
    • 77955616558 scopus 로고    scopus 로고
    • Compartmentalization of mammalian folatemediated one-carbon metabolism
    • A.S. Tibbetts, D.R. Appling, Compartmentalization of mammalian folatemediated one-carbon metabolism, Annu. Rev. Nutr. 30 (2010) 57-81.
    • (2010) Annu. Rev. Nutr. , vol.30 , pp. 57-81
    • Tibbetts, A.S.1    Appling, D.R.2
  • 7
    • 0002162964 scopus 로고    scopus 로고
    • Folate biochemistry in relation to antifolate selectivity
    • A.L. Jackman (Ed.) Humana Press, Totowa, NJ
    • R.L. Kisliuk, Folate biochemistry in relation to antifolate selectivity, in: A.L. Jackman (Ed.), Antifolate Drugs in Cancer Therapy, Humana Press, Totowa, NJ, 1999, pp. 13-36.
    • (1999) Antifolate Drugs in Cancer Therapy , pp. 13-36
    • Kisliuk, R.L.1
  • 8
    • 59049107134 scopus 로고    scopus 로고
    • FDH: An aldehyde dehydrogenase fusion enzyme in folate metabolism
    • S.A. Krupenko, FDH: an aldehyde dehydrogenase fusion enzyme in folate metabolism, Chem. Biol. Interact. 178 (1-3) (2009) 84-93.
    • (2009) Chem. Biol. Interact. , vol.178 , Issue.1-3 , pp. 84-93
    • Krupenko, S.A.1
  • 9
    • 0035998275 scopus 로고    scopus 로고
    • 10-Formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in tumor tissues and possesses suppressor effects on cancer cells
    • S.A. Krupenko, N.V. Oleinik, 10-formyltetrahydrofolate dehydrogenase, one of the major folate enzymes, is down-regulated in tumor tissues and possesses suppressor effects on cancer cells, Cell Growth Differ. 13 (5) (2002) 227-236.
    • (2002) Cell Growth Differ. , vol.13 , Issue.5 , pp. 227-236
    • Krupenko, S.A.1    Oleinik, N.V.2
  • 11
    • 0030942262 scopus 로고    scopus 로고
    • Domain structure of rat 10-formyltetrahydrofolate dehydrogenase: Resolution of the amino-terminal domain as 10-formyltetrahydrofolate hydrolase
    • DOI 10.1074/jbc.272.15.10273
    • S.A. Krupenko, C. Wagner, R.J. Cook, Domain structure of rat 10- formyltetrahydrofolate dehydrogenase. Resolution of the amino-terminal domain as 10-formyltetrahydrofolate hydrolase, J. Biol. Chem. 272 (15) (1997) 10273-10278. (Pubitemid 27171709)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.15 , pp. 10273-10278
    • Krupenko, S.A.1    Wagner, C.2    Cook, R.J.3
  • 12
    • 0030950437 scopus 로고    scopus 로고
    • Expression, purification, and properties of the aldehyde dehydrogenase homologous carboxyl-terminal domain of rat 10-formyltetrahydrofolate dehydrogenase
    • DOI 10.1074/jbc.272.15.10266
    • S.A. Krupenko, C. Wagner, R.J. Cook, Expression, purification, and properties of the aldehyde dehydrogenase homologous carboxyl-terminal domain of rat 10-formyltetrahydrofolate dehydrogenase, J. Biol. Chem. 272 (15) (1997) 10266-10272. (Pubitemid 27171708)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.15 , pp. 10266-10272
    • Krupenko, S.A.1    Wagner, C.2    Cook, R.J.3
  • 13
    • 36048947884 scopus 로고    scopus 로고
    • 10-Formyltetrahydrofolate dehydrogenase requires a 4′- phosphopantetheine prosthetic group for catalysis
    • H. Donato, N.I. Krupenko, Y. Tsybovsky, S.A. Krupenko, 10-formyltetrahydrofolate dehydrogenase requires a 4′-phosphopantetheine prosthetic group for catalysis, J. Biol. Chem. 282 (47) (2007) 34159-34166.
    • (2007) J. Biol. Chem. , vol.282 , Issue.47 , pp. 34159-34166
    • Donato, H.1    Krupenko, N.I.2    Tsybovsky, Y.3    Krupenko, S.A.4
  • 14
    • 76249106733 scopus 로고    scopus 로고
    • Acyl carrier protein-specific 4′-phosphopantetheinyl transferase activates 10-formyltetrahydrofolate dehydrogenase
    • K.C. Strickland, L.A. Hoeferlin, N.V. Oleinik, N.I. Krupenko, S.A. Krupenko, Acyl carrier protein-specific 4′-phosphopantetheinyl transferase activates 10-formyltetrahydrofolate dehydrogenase, J. Biol. Chem. 285 (3) (2010) 1627-1633.
    • (2010) J. Biol. Chem. , vol.285 , Issue.3 , pp. 1627-1633
    • Strickland, K.C.1    Hoeferlin, L.A.2    Oleinik, N.V.3    Krupenko, N.I.4    Krupenko, S.A.5
  • 16
    • 0028911866 scopus 로고
    • Recombinant 10-formyltetrahydrofolate dehydrogenase catalyses both dehydrogenase and hydrolase reactions utilizing the synthetic substrate 10-formyl-5,8-dideazafolate
    • S.A. Krupenko, C. Wagner, R.J. Cook, Recombinant 10- formyltetrahydrofolate dehydrogenase catalyses both dehydrogenase and hydrolase reactions utilizing the synthetic substrate 10-formyl-5,8-dideazafolate, Biochem. J. 306 (Pt 3) (1995) 651-655.
    • (1995) Biochem. J. , vol.306 , Issue.PART 3 , pp. 651-655
    • Krupenko, S.A.1    Wagner, C.2    Cook, R.J.3
  • 17
    • 0033544874 scopus 로고    scopus 로고
    • Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase
    • S.A. Krupenko, C. Wagner, Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase, J. Biol. Chem. 274 (50) (1999) 35777-35784.
    • (1999) J. Biol. Chem. , vol.274 , Issue.50 , pp. 35777-35784
    • Krupenko, S.A.1    Wagner, C.2
  • 18
    • 0019878597 scopus 로고
    • Nicotinamide adenine dinucleotide activation of the esterase reaction of horse liver aldehyde dehydrogenase
    • K. Takahashi, H. Weiner, Nicotinamide adenine dinucleotide activation of the esterase reaction of horse liver aldehyde dehydrogenase, Biochemistry 20 (10) (1981) 2720-2726.
    • (1981) Biochemistry , vol.20 , Issue.10 , pp. 2720-2726
    • Takahashi, K.1    Weiner, H.2
  • 19
    • 0029133305 scopus 로고
    • Enzymatic activities of rat liver cytosol 10- Formyltetrahydrofolate dehydrogenase
    • R.J. Cook, C. Wagner, Enzymatic activities of rat liver cytosol 10- formyltetrahydrofolate dehydrogenase, Arch. Biochem. Biophys. 321 (2) (1995) 336-344.
    • (1995) Arch. Biochem. Biophys. , vol.321 , Issue.2 , pp. 336-344
    • Cook, R.J.1    Wagner, C.2
  • 21
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • DOI 10.1093/nar/gkg520
    • T. Schwede, J. Kopp, N. Guex, M.C. Peitsch, SWISS-MODEL: an automated protein homology-modeling server, Nucleic Acids Res. 31 (13) (2003) 3381-3385. (Pubitemid 37442164)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 22
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • E. Krissinel, K. Henrick, 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.PART 12 AND PART 1 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 23
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D: Biol. Crystallogr. 50 (Pt 5) (1994) 760-763.
    • (1994) Acta Crystallogr. D: Biol. Crystallogr. , vol.50 , Issue.PART 5 , pp. 760-763
  • 24
    • 0042858246 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a human 4′ -phosphopantetheinyl transferase with broad substrate specificity
    • DOI 10.1074/jbc.M305459200
    • A.K. Joshi, L. Zhang, V.S. Rangan, S. Smith, Cloning, expression, and characterization of a human 4′-phosphopantetheinyl transferase with broad substrate specificity, J. Biol. Chem. 278 (35) (2003) 33142-33149. (Pubitemid 37055761)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.35 , pp. 33142-33149
    • Joshi, A.K.1    Zhang, L.2    Rangan, V.S.3    Smith, S.4
  • 26
    • 1842740027 scopus 로고    scopus 로고
    • The crystal structure of the hydrolase domain of 10- formyltetrahydrofolate dehydrogenase: Mechanism of hydrolysis and its interplay with the dehydrogenase domain
    • A.A. Chumanevich, S.A. Krupenko, C. Davies, The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase: mechanism of hydrolysis and its interplay with the dehydrogenase domain, J. Biol. Chem. 279 (14) (2004) 14355-14364.
    • (2004) J. Biol. Chem. , vol.279 , Issue.14 , pp. 14355-14364
    • Chumanevich, A.A.1    Krupenko, S.A.2    Davies, C.3
  • 27
    • 33947424367 scopus 로고    scopus 로고
    • Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: Implications for the catalytic mechanism of aldehyde dehydrogenases
    • DOI 10.1021/bi0619573
    • Y. Tsybovsky, H. Donato, N.I. Krupenko, C. Davies, S.A. Krupenko, Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases, Biochemistry 46 (11) (2007) 2917-2929. (Pubitemid 46449116)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 2917-2929
    • Tsybovsky, Y.1    Donato, H.2    Krupenko, N.I.3    Davies, C.4    Krupenko, S.A.5
  • 28
    • 0028938730 scopus 로고
    • Cysteine 707 is involved in the dehydrogenase activity site of rat 10-formyltetrahydrofolate dehydrogenase
    • S.A. Krupenko, C. Wagner, R.J. Cook, Cysteine 707 is involved in the dehydrogenase activity site of rat 10-formyltetrahydrofolate dehydrogenase, J. Biol. Chem. 270 (2) (1995) 519-522.
    • (1995) J. Biol. Chem. , vol.270 , Issue.2 , pp. 519-522
    • Krupenko, S.A.1    Wagner, C.2    Cook, R.J.3
  • 29
    • 0035968161 scopus 로고    scopus 로고
    • On the role of conserved histidine 106 in 10-formyltetrahydrofolate dehydrogenase catalysis: Connection between hydrolase and dehydrogenase mechanisms
    • S.A. Krupenko, A.P. Vlasov, C. Wagner, On the role of conserved histidine 106 in 10-formyltetrahydrofolate dehydrogenase catalysis: connection between hydrolase and dehydrogenase mechanisms, J. Biol. Chem. 276 (26) (2001) 24030-24037.
    • (2001) J. Biol. Chem. , vol.276 , Issue.26 , pp. 24030-24037
    • Krupenko, S.A.1    Vlasov, A.P.2    Wagner, C.3
  • 30
    • 21844446870 scopus 로고    scopus 로고
    • Glutathione redox state regulates mitochondrial reactive oxygen production
    • D. Shen, T.P. Dalton, D.W. Nebert, H.G. Shertzer, Glutathione redox state regulates mitochondrial reactive oxygen production, J. Biol. Chem. 280 (27) (2005) 25305-25312.
    • (2005) J. Biol. Chem. , vol.280 , Issue.27 , pp. 25305-25312
    • Shen, D.1    Dalton, T.P.2    Nebert, D.W.3    Shertzer, H.G.4
  • 31
    • 0015499994 scopus 로고
    • Horse liver aldehyde dehydrogenase. II. Kinetics and mechanistic implications of the dehydrogenase and esterase activity
    • R.I. Feldman, H. Weiner, Horse liver aldehyde dehydrogenase. II. Kinetics and mechanistic implications of the dehydrogenase and esterase activity, J. Biol. Chem. 247 (1) (1972) 267-272.
    • (1972) J. Biol. Chem. , vol.247 , Issue.1 , pp. 267-272
    • Feldman, R.I.1    Weiner, H.2
  • 32
    • 0030811549 scopus 로고    scopus 로고
    • The potential roles of the conserved amino acids in human liver mitochondrial aldehyde dehydrogenase
    • S. Sheikh, L. Ni, T.D. Hurley, H. Weiner, The potential roles of the conserved amino acids in human liver mitochondrial aldehyde dehydrogenase, J. Biol. Chem. 272 (30) (1997) 18817-18822.
    • (1997) J. Biol. Chem. , vol.272 , Issue.30 , pp. 18817-18822
    • Sheikh, S.1    Ni, L.2    Hurley, T.D.3    Weiner, H.4
  • 33
    • 0035969894 scopus 로고    scopus 로고
    • Chemical mechanism and substrate binding sites of NADP-dependent aldehyde dehydrogenase from Streptococcus mutans
    • DOI 10.1016/S0009-2797(00)00218-0, PII S0009279700002180
    • S. Marchal, D. Cobessi, S. Rahuel-Clermont, F. Tete-Favier, A. Aubry, G. Branlant, Chemical mechanism and substrate binding sites of NADP-dependent aldehyde dehydrogenase from Streptococcus mutans, Chem. Biol. Interact. 130-132 (1-3) (2001) 15-28. (Pubitemid 32295799)
    • (2001) Chemico-Biological Interactions , vol.130-132 , pp. 15-28
    • Marchal, S.1    Cobessi, D.2    Rahuel-Clermont, S.3    Tete-Favier, F.4    Aubry, A.5    Branlant, G.6
  • 34
    • 77956219280 scopus 로고    scopus 로고
    • Zebrafish 10-formyltetrahydrofolate dehydrogenase is similar to its mammalian isozymes for its structural and catalytic properties
    • W.N. Chang, H.C. Lin, T.F. Fu, Zebrafish 10-formyltetrahydrofolate dehydrogenase is similar to its mammalian isozymes for its structural and catalytic properties, Protein Expr. Purif. 72 (2) (2010) 217-222.
    • (2010) Protein Expr. Purif. , vol.72 , Issue.2 , pp. 217-222
    • Chang, W.N.1    Lin, H.C.2    Fu, T.F.3
  • 35
    • 0035969884 scopus 로고    scopus 로고
    • Order and disorder in mitochondrial aldehyde dehydrogenase
    • DOI 10.1016/S0009-2797(00)00217-9, PII S0009279700002179
    • T.D. Hurley, S. Perez-Miller, H. Breen, Order and disorder in mitochondrial aldehyde dehydrogenase, Chem. Biol. Interact. 130-132 (1-3) (2001) 3-14. (Pubitemid 32295798)
    • (2001) Chemico-Biological Interactions , vol.130-132 , pp. 3-14
    • Hurley, T.D.1    Perez-Miller, S.2    Breen, H.3
  • 37
    • 0028961395 scopus 로고
    • Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis
    • J. Farres, T.T. Wang, S.J. Cunningham, H. Weiner, Investigation of the active site cysteine residue of rat liver mitochondrial aldehyde dehydrogenase by site-directed mutagenesis, Biochemistry 34 (8) (1995) 2592-2598.
    • (1995) Biochemistry , vol.34 , Issue.8 , pp. 2592-2598
    • Farres, J.1    Wang, T.T.2    Cunningham, S.J.3    Weiner, H.4
  • 38
  • 40
    • 0023789244 scopus 로고
    • In vitro evidence for the involvement of mitochondrial folate metabolism in the supply of cytoplasmic one-carbon units
    • C.K. Barlowe, D.R. Appling, In vitro evidence for the involvement of mitochondrial folate metabolism in the supply of cytoplasmic one-carbon units, Biofactors 1 (2) (1988) 171-176.
    • (1988) Biofactors , vol.1 , Issue.2 , pp. 171-176
    • Barlowe, C.K.1    Appling, D.R.2
  • 41
    • 0027160524 scopus 로고
    • Characterization of the folate-dependent mitochondrial oxidation of carbon 3 of serine
    • L.F. Garcia-Martinez, D.R. Appling, Characterization of the folate-dependent mitochondrial oxidation of carbon 3 of serine, Biochemistry 32 (17) (1993) 4671-4676. (Pubitemid 23143259)
    • (1993) Biochemistry , vol.32 , Issue.17 , pp. 4671-4676
    • Garcia-Martinez, L.F.1    Appling, D.R.2
  • 42
    • 0014692346 scopus 로고
    • The presence of N-formyl-methionyl-tRNA in HeLa cell mitochondria
    • J.B. Galper, J.E. Darnell, The presence of N-formyl-methionyl-tRNA in HeLa cell mitochondria, Biochem. Biophys. Res. Commun. 34 (2) (1969) 205-214.
    • (1969) Biochem. Biophys. Res. Commun. , vol.34 , Issue.2 , pp. 205-214
    • Galper, J.B.1    Darnell, J.E.2
  • 43
    • 0015011935 scopus 로고
    • Isolation of Saccharomyces cerevisiae mitochondrial formyltetrahydrofolic acid:methionyl-tRNA transformylase and the hybridization of mitochondrial fMet-tRNA with mitochondrial DNA
    • A. Halbreich, M. Rabinowitz, Isolation of Saccharomyces cerevisiae mitochondrial formyltetrahydrofolic acid:methionyl-tRNA transformylase and the hybridization of mitochondrial fMet-tRNA with mitochondrial DNA, Proc. Natl. Acad. Sci. U.S.A. 68 (2) (1971) 294-298.
    • (1971) Proc. Natl. Acad. Sci. U.S.A. , vol.68 , Issue.2 , pp. 294-298
    • Halbreich, A.1    Rabinowitz, M.2


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