메뉴 건너뛰기




Volumn 43, Issue 33, 2004, Pages 10692-10700

Role of glycine 81 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate specificity and oxidase activity

Author keywords

[No Author keywords available]

Indexed keywords

ACIDS; MOLECULAR DYNAMICS; OXIDATION; OXYGEN; REACTION KINETICS; SUBSTRATES;

EID: 4143117810     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049005p     Document Type: Article
Times cited : (18)

References (36)
  • 1
    • 0025013451 scopus 로고
    • Mandelate pathway of Pseudomonas putida: Sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli
    • Tsou, A. Y., Ransom, S. C., Gerlt, J. A., Buechter, D. D., Babbitt, P. C., and Kenyon, G. L. (1990) Mandelate pathway of Pseudomonas putida: Sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli, Biochemistry 29, 9856-9862.
    • (1990) Biochemistry , vol.29 , pp. 9856-9862
    • Tsou, A.Y.1    Ransom, S.C.2    Gerlt, J.A.3    Buechter, D.D.4    Babbitt, P.C.5    Kenyon, G.L.6
  • 2
    • 0025786780 scopus 로고
    • Amino acid sequence of long chain α-hydroxy acid oxidase from rat kidney, a member of the family of FMN-dependent α-hydroxy acid-oxidizing enzymes
    • Diêp Le, K. H., and Lederer, F. (1991) Amino acid sequence of long chain α-hydroxy acid oxidase from rat kidney, a member of the family of FMN-dependent α-hydroxy acid-oxidizing enzymes, J. Biol. Chem. 266, 20877-20881.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20877-20881
    • Diêp Le, K.H.1    Lederer, F.2
  • 4
    • 0015524246 scopus 로고
    • Mechanism of action of the flavoenzyme lactate oxidase
    • Lockridge, O., Massey, V., and Sullivan, P. A. (1972) Mechanism of action of the flavoenzyme lactate oxidase, J. Biol. Chem. 247, 8097-8106.
    • (1972) J. Biol. Chem. , vol.247 , pp. 8097-8106
    • Lockridge, O.1    Massey, V.2    Sullivan, P.A.3
  • 5
    • 0022539540 scopus 로고
    • D-lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase
    • Matsushita, K., and Kaback, H. R. (1986) D-Lactate oxidation and generation of the proton electrochemical gradient in membrane vesicles from Escherichia coli GR19N and in proteoliposomes reconstituted with purified D-lactate dehydrogenase and cytochrome o oxidase, Biochemistry 25, 2321-2327.
    • (1986) Biochemistry , vol.25 , pp. 2321-2327
    • Matsushita, K.1    Kaback, H.R.2
  • 6
    • 0027358810 scopus 로고
    • Three overlapping 1ct genes involved in L-lactate utilization by Escherichia coli
    • Dong, J. M., Taylor, J. S., Latour, D. J., Iuchi, S., and Lin, E. C. C. (1993) Three overlapping 1ct genes involved in L-lactate utilization by Escherichia coli, J. Bacteriol. 175, 6671-6678.
    • (1993) J. Bacteriol. , vol.175 , pp. 6671-6678
    • Dong, J.M.1    Taylor, J.S.2    Latour, D.J.3    Iuchi, S.4    Lin, E.C.C.5
  • 7
    • 0024962365 scopus 로고
    • Refined structure of spinach glycolate oxidase at 2 Å resolution
    • Lindqvist, Y. (1989) Refined structure of spinach glycolate oxidase at 2 Å resolution, J. Mol. Biol. 209, 151-166.
    • (1989) J. Mol. Biol. , vol.209 , pp. 151-166
    • Lindqvist, Y.1
  • 9
    • 0025853478 scopus 로고
    • 2 are structurally homologous and evolutionarily related enzymes with distinctly different function and flavin mononucleotide binding
    • 2 are structurally homologous and evolutionarily related enzymes with distinctly different function and flavin mononucleotide binding, J. Biol. Chem. 266, 3198-3207.
    • (1991) J. Biol. Chem. , vol.266 , pp. 3198-3207
    • Lindqvist, Y.1    Brändén, C.-I.2    Mathews, F.S.3    Lederer, F.4
  • 10
    • 0035928723 scopus 로고    scopus 로고
    • Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase
    • Sukumar, N., Xu, Y., Gatti, D. L., Mitra B., and Mathews, F. S. (2001) Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase, Biochemistry 40, 9870-9878.
    • (2001) Biochemistry , vol.40 , pp. 9870-9878
    • Sukumar, N.1    Xu, Y.2    Gatti, D.L.3    Mitra, B.4    Mathews, F.S.5
  • 11
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproterns
    • Massey, V. (1994) Activation of molecular oxygen by flavins and flavoproterns, J. Biol. Chem. 269, 22459-22462.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 12
    • 0033592410 scopus 로고    scopus 로고
    • A highly active, soluble mutant of the membrane-associated (S)-mandelate dehydrogenase from Pseudomonas putida
    • Xu, Y., and Mitra, B. (1999) A highly active, soluble mutant of the membrane-associated (S)-mandelate dehydrogenase from Pseudomonas putida, Biochemistry 38, 12367-12376.
    • (1999) Biochemistry , vol.38 , pp. 12367-12376
    • Xu, Y.1    Mitra, B.2
  • 14
    • 0029911191 scopus 로고    scopus 로고
    • Conversion of L-lactate oxidase to a long chain α-hydroxyacid oxidase by site-directed mutagenesis of alanine 95 to glycine
    • Yorita, K., Aki, K., Ohkuma-Soyejima, T., Kokubo, T., Misaki, H., and Massey, V. (1996) Conversion of L-lactate oxidase to a long chain α-hydroxyacid oxidase by site-directed mutagenesis of alanine 95 to glycine, J. Biol. Chem. 271, 28300-28305.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28300-28305
    • Yorita, K.1    Aki, K.2    Ohkuma-Soyejima, T.3    Kokubo, T.4    Misaki, H.5    Massey, V.6
  • 15
    • 0030035112 scopus 로고    scopus 로고
    • Site-directed mutagenesis of glycine 99 to alanine in L-lactate monooxygenase from Mycobacterium smegmatis
    • Sun, W., Williams, C. H., and Massey, V. (1996) Site-directed mutagenesis of glycine 99 to alanine in L-lactate monooxygenase from Mycobacterium smegmatis, J. Biol. Chem. 271, 17226-17233.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17226-17233
    • Sun, W.1    Williams, C.H.2    Massey, V.3
  • 16
    • 0030827996 scopus 로고    scopus 로고
    • The role of glycine 99 in L-lactate monooxygenase from Mycobacterium smegmatis
    • Sun, W., Williams, C. H., and Massey, V. (1997) The role of glycine 99 in L-lactate monooxygenase from Mycobacterium smegmatis, J. Biol. Chem. 272, 27065-27076.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27065-27076
    • Sun, W.1    Williams, C.H.2    Massey, V.3
  • 17
    • 0026002950 scopus 로고
    • Mechanism of the reaction catalyzed by mandelate racemase. 3. Asymmetry in reactions catalyzed by the H297N mutant
    • Landro, J. A., Kallarakal, A. T., Ransom, S. C., Gerlt, J. A., Kozarich, J. W., Neidhart, D. J., and Kenyon, G. L. (1991) Mechanism of the reaction catalyzed by mandelate racemase. 3. Asymmetry in reactions catalyzed by the H297N mutant, Biochemistry 30, 9274-9281.
    • (1991) Biochemistry , vol.30 , pp. 9274-9281
    • Landro, J.A.1    Kallarakal, A.T.2    Ransom, S.C.3    Gerlt, J.A.4    Kozarich, J.W.5    Neidhart, D.J.6    Kenyon, G.L.7
  • 18
    • 0033522475 scopus 로고    scopus 로고
    • (S)-mandelate dehydrogenase from Pseudomonas putida: Mechanistic studies with alternate substrates and pH and kinetic isotope effects
    • Lehoux, I. E., and Mitra, B. (1999) (S)-Mandelate dehydrogenase from Pseudomonas putida: Mechanistic studies with alternate substrates and pH and kinetic isotope effects, Biochemistry 38, 5836-5848.
    • (1999) Biochemistry , vol.38 , pp. 5836-5848
    • Lehoux, I.E.1    Mitra, B.2
  • 19
    • 0002435359 scopus 로고
    • A simple method for the determination of redox potentials
    • (Curti, B., et al., Eds.), Walter de Gruyter, New York
    • Massey, V. (1991) A simple method for the determination of redox potentials, in Flavins and Flavoproteins, (Curti, B., et al., Eds.) pp 59-66, Walter de Gruyter, New York.
    • (1991) Flavins and Flavoproteins , pp. 59-66
    • Massey, V.1
  • 20
    • 0017810568 scopus 로고
    • Determination of glucose oxidase oxidation-reduction potentials and the oxygen reactivity of fully reduced and semiquinoid forms
    • Stankovich, M. T., Schopfer, L. M., and Massey, V. (1978) Determination of glucose oxidase oxidation-reduction potentials and the oxygen reactivity of fully reduced and semiquinoid forms, J. Biol. Chem. 253, 4971-4979.
    • (1978) J. Biol. Chem. , vol.253 , pp. 4971-4979
    • Stankovich, M.T.1    Schopfer, L.M.2    Massey, V.3
  • 21
    • 0242424115 scopus 로고    scopus 로고
    • A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida
    • Dewanti, A. R., and Mitra, B. (2003) A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida, Biochemistry 42, 12893-12901.
    • (2003) Biochemistry , vol.42 , pp. 12893-12901
    • Dewanti, A.R.1    Mitra, B.2
  • 22
    • 0025741770 scopus 로고
    • Expression of spinach glycolate oxidase in Saccharomyces cerevisiae: Purification and characterization
    • Macheroux, P., Massey, V., Thiele, D. J., and Volokita, M. (1991) Expression of spinach glycolate oxidase in Saccharomyces cerevisiae: Purification and characterization, Biochemistry 30, 4612-4619.
    • (1991) Biochemistry , vol.30 , pp. 4612-4619
    • Macheroux, P.1    Massey, V.2    Thiele, D.J.3    Volokita, M.4
  • 24
    • 0025819901 scopus 로고
    • Reactivity of medium-chain acyl-CoA dehydrogenase toward molecular oxygen
    • Wang, R., and Thorpe, C. (1991) Reactivity of medium-chain acyl-CoA dehydrogenase toward molecular oxygen, Biochemistry 30, 7895-7901.
    • (1991) Biochemistry , vol.30 , pp. 7895-7901
    • Wang, R.1    Thorpe, C.2
  • 25
    • 0029953886 scopus 로고    scopus 로고
    • Crystal structure of flavodoxin from Desulfovibrio desulfuricans ATCC 27774 in two oxidation states
    • Romero, A., Caldeira, J., Legall, J., Moura, I., Moura, J. J., and Romao, M. J. (1996) Crystal structure of flavodoxin from Desulfovibrio desulfuricans ATCC 27774 in two oxidation states, Eur. J. Biochem. 239, 190-196.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 190-196
    • Romero, A.1    Caldeira, J.2    Legall, J.3    Moura, I.4    Moura, J.J.5    Romao, M.J.6
  • 26
    • 0031024423 scopus 로고    scopus 로고
    • Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: The role of conformation changes
    • Ludwig, M. L., Pattridge, K. A., Metzger, A. L., Dixon, M. M., Eren, M., Feng, Y., and Swenson, R. P. (1997) Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: The role of conformation changes, Biochemistry 36, 1259-1280.
    • (1997) Biochemistry , vol.36 , pp. 1259-1280
    • Ludwig, M.L.1    Pattridge, K.A.2    Metzger, A.L.3    Dixon, M.M.4    Eren, M.5    Feng, Y.6    Swenson, R.P.7
  • 27
    • 0035856536 scopus 로고    scopus 로고
    • Alanine-scanning of the 50's loop in the Clostridium beijerinckii flavodoxin: Evaluation of additivity and the importance of interactions provided by the main chain in the modulation of the oxidation-reduction potentials
    • Kasim, M., and Swenson, R. P. (2001) Alanine-scanning of the 50's loop in the Clostridium beijerinckii flavodoxin: Evaluation of additivity and the importance of interactions provided by the main chain in the modulation of the oxidation-reduction potentials, Biochemistry 40, 13548-13555.
    • (2001) Biochemistry , vol.40 , pp. 13548-13555
    • Kasim, M.1    Swenson, R.P.2
  • 28
    • 0942265528 scopus 로고    scopus 로고
    • High-resolution structures of an oxidized and reduced flavoprotein: The water switch in a soluble form of (S)-mandelate dehydrogenase
    • Sukumar, N., Dewanti, A. R., Mitra, B., and Mathew, F. S. (2004) High-resolution structures of an oxidized and reduced flavoprotein: The water switch in a soluble form of (S)-mandelate dehydrogenase, J. Biol. Chem. 279, 3749-3757.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3749-3757
    • Sukumar, N.1    Dewanti, A.R.2    Mitra, B.3    Mathew, F.S.4
  • 29
    • 0014670427 scopus 로고
    • Flavin-sulfite complexes and their structures
    • Muller, F., and Massey, V. (1969) Flavin-sulfite complexes and their structures, J. Biol. Chem. 244, 4007-4016.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4007-4016
    • Muller, F.1    Massey, V.2
  • 31
    • 0023665350 scopus 로고
    • The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone
    • Volokita, M., and Somerville, C. R. (1987) The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone, J. Biol. Chem. 262, 15825-15828.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15825-15828
    • Volokita, M.1    Somerville, C.R.2
  • 32
    • 0034725053 scopus 로고    scopus 로고
    • Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases
    • Jones, J. M., Morrell, J. C., and Gould, S. (2000) Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases, J. Biol. Chem. 275, 12590-12597.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12590-12597
    • Jones, J.M.1    Morrell, J.C.2    Gould, S.3
  • 33
    • 0028817797 scopus 로고
    • L-lactate oxidase and L-lactate monooxygenase: Mechanistic variations on a common structural theme
    • Maeda-Yorita, K., Aki, K., Sagai, H., Misaki, H., and Massey, V. (1995) L-Lactate oxidase and L-lactate monooxygenase: Mechanistic variations on a common structural theme, Biochimie 77, 631-642.
    • (1995) Biochimie , vol.77 , pp. 631-642
    • Maeda-Yorita, K.1    Aki, K.2    Sagai, H.3    Misaki, H.4    Massey, V.5
  • 34
  • 36
    • 0032127918 scopus 로고    scopus 로고
    • L-mandelate dehydrogenase from Rhodotorula graminis: Cloning, sequencing, and kinetic characterization of the recombinant enzyme and its independently expressed flavin domain
    • Illias, R. M., Sinclair, R., Robertson, D., Neu, A., Chapman, S. K., and Reid, G. A. (1998) L-Mandelate dehydrogenase from Rhodotorula graminis: Cloning, sequencing, and kinetic characterization of the recombinant enzyme and its independently expressed flavin domain, Biochem. J. 333, 107-115.
    • (1998) Biochem. J. , vol.333 , pp. 107-115
    • Illias, R.M.1    Sinclair, R.2    Robertson, D.3    Neu, A.4    Chapman, S.K.5    Reid, G.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.