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0.02
-
wild type enzyme with ferricyanide as electron acceptor
8.5
-
A198G/L230G mutant enzyme with ferricyanide as electron acceptor
0.0033
-
wild-type, pH 7.0, 25°C
6.6
-
mutant A95G, pH 7.0, 25°C
15.8
-
mutant A95G, pH 7.0, 25°C
1.2
-
at pH 7.5 and 28°C
0.04
-
pH 7.5, 20°C, mutant enzyme R165G/R277K
0.05
-
pH 7.5, 20°C, mutant enzyme G81V
0.09
-
mutant enzyme H274G, in presence of 20 mM imidazole
0.11
-
pH 7.5, 20°C, mutant enzyme G81D
0.23
-
mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5
0.23
-
pH 7.5, 20°C, mutant enzyme R277G
0.27
-
pH 7.5, 20°C, mutant enzyme R277L
0.64
-
pH 7.5, 20°C, mutant enzyme R277G
1.1
-
pH 7.5, 20°C, mutant enzyme R165K/R277K
1.52
-
pH 7.5, 20°C, mutant enzyme R277H
1.6
-
pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach
2.3
-
pH 7.5, 20°C, mutant enzyme, G81A/MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach and a G81A mutation in MDH
2.8
-
pH 7.5, 20°C, mutant enzyme G81S
3
6
pH 7.5, 25°C, electron acceptor: 2,6-dichloroindophenol
4.4
-
pH 7.5, 20°C, mutant enzyme R165E
9
-
pH 7.5, (S)-mandelate dehydrogenase with residues 2-4 deleted
13.2
-
pH 7.5, 20°C, mutant enzyme R165G
18.4
-
pH 7.5, 20°C, mutant enzyme R165M
19.2
-
pH 7.5, 20°C, mutant enzyme G81A
24
-
pH 7.5, (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus
49
-
pH 7.5, 25°C, electron acceptor: cytochrome c
66
-
mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5
66
-
pH 7.5, 20°C, mutant enzyme R277K
73
-
pH 7.5, 20°C, mutant enzyme R277K
109
-
pH 7.5, 25°C, electron acceptor: ferricyanide
114
-
pH 7.5, 25°C, cosubstrate: ferricyanide
120
-
pH 7.5, 20°C, mutant enzyme R165K
174
-
pH 7.5, wild-type enzyme
205
-
pH 7.5, 20°C, cosubstrate: 2,6-dichloroindophenol, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
205
-
pH 7.5, 20°C, mutant enzyme MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with 205 residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
270
-
pH 7.5, 20°C, wild-type enzyme
290
-
pH 7.5, 20°C, cosubstrate: 2,6-dichloroindophenol, wild-type enzyme
360
-
pH 7.5, 20°C, wild-type enzyme
360
-
wild type enzyme, at 20°C, in 0.1 M potassium phosphate, pH 7.5
2.5
-
25°C, pH 7.5, mutant enzyme N197A
12
-
mutant enzyme F52W/Y64W
22
-
mutant A25V, pH 7.5, 25°C
22
-
mutant V26F, pH 7.5, 25°C
22
-
pH 7.5, 3.3 mM Mg2+, mutant A25V
22
-
pH 7.5, 3.3 mM Mg2+, mutant V26F
23
-
mutant V26L, pH 7.5, 25°C
23
-
pH 7.5, 3.3 mM Mg2+, mutant V26L
53
-
mutant V29F, pH 7.5, 25°C
53
-
pH 7.5, 3.3 mM Mg2+, mutant V29F
77
-
mutant V22A, pH 7.5, 25°C
77
-
pH 7.5, 3.3 mM Mg2+ mutant V22A
89
-
mutant V26A/V29L, pH 7.5, 25°C
89
-
pH 7.5, 3.3 mM Mg2+, mutant V26A/V29L
98
-
mutant V22F, pH 7.5, 25°C
98
-
pH 7.5, 3.3 mM Mg2+, mutant V22F
120
-
mutant T24S, pH 7.5, 25°C
120
-
pH 7.5, 3.3 mM Mg2+, mutant T24S
176
-
mutant V29A, pH 7.5, 25°C
176
-
pH 7.5, 3.3 mM Mg2+, mutant V29A
180
-
mutant V29L, pH 7.5, 25°C
180
-
pH 7.5, 3.3 mM Mg2+, mutant V29L
190
-
recombinant mandelate racemase, putative misfolded form with N-terminal hexahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
447
-
25°C, pH 7.5, wild-type enzyme
470
-
pH 7.5, 3.3 mM Mg2+, wild-type
470
-
wild-type, pH 7.5, 25°C
472
-
recombinant mandelate racemase fusion protein bearing an N-terminal StrepII-tag and a C-terminal decahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
492
-
pH 7.5, 20 mM Mg2+, wild-type
492
-
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
550
-
mutant V26A, pH 7.5, 25°C
550
-
pH 7.5, 3.3 mM Mg2+, mutant V26A
637
-
pH 7.5, 25°C, recombinant wild-type enzyme
710
-
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
710
-
pH 7.5, 3.3 mM Mg2+, mutant V26A/V29L
740
-
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
740
-
pH 7.5, 3.3 mM Mg2+, mutant V22I
940
-
recombinant mandelate racemase represents correctly folded enzyme, with N-terminal hexahistidine tag, in Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
1124
-
recombinant enzyme replacement of the N-terminal hexahistidine tag by a StrepII-tag appears to ameliorate the folding problem yielding a single enzyme species, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
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0.3
-
wild-type, pH 7.0, 25°C
20
-
mutant A95G, pH 7.0, 25°C
0.04
-
pH 7.5, 20°C, mutant enzyme, G81A/MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach and a G81A mutation in MDH
0.085
-
pH 7.5, 20°C, cosubstrate: 2,6-dichloroindophenol, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.09
-
pH 7.5, 20°C, mutant enzyme MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach
0.12
-
pH 7.5, 20°C, wild-type enzyme
0.12
-
wild type enzyme, at 20°C, in 0.1 M potassium phosphate, pH 7.5
0.13
-
pH 7.5, 20°C, wild-type enzyme
0.15
-
pH 7.5, 20°C, mutant enzyme G81A
0.158
-
pH 7.5, (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus
0.17
-
pH 7.5, 20°C, mutant enzyme G81V
0.18
-
pH 7.5, 20°C, cosubstrate: 2,6-dichloroindophenol, wild-type enzyme
0.18
-
pH 7.5, 25°C, electron acceptor: 2,6-dichloroindophenol
0.206
-
pH 7.5, wild-type enzyme
0.225
-
pH 7.5, (S)-mandelate dehydrogenase with residues 2-4 deleted
0.229
-
pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach
0.24
-
pH 7.5, 25°C, cosubstrate: ferricyanide
0.27
-
chitosan-immobilized enzyme, at pH 3.4 and 45°C
0.27
-
pH 7.5, 25°C, electron acceptor: ferricyanide
0.49
-
pH 7.5, 25°C, electron acceptor: cytochrome c
0.92
-
at pH 6.5 and 30°C
1.5
-
pH 7.5, 20°C, mutant enzyme R165K
2
-
pH 7.5, 20°C, mutant enzyme G81D
2.3
-
pH 7.5, 20°C, mutant enzyme G81S
4.4
-
pH 7.5, 20°C, mutant enzyme R165M
4.4
-
pH 7.5, 20°C, mutant enzyme R277K
5.6
-
mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5
5.6
-
pH 7.5, 20°C, mutant enzyme R277K
5.8
-
pH 7.5, 20°C, mutant enzyme R165G
12
-
pH 7.5, 20°C, mutant enzyme R165E
13
-
mutant enzyme H274G, in presence of 20 mM imidazole
15.2
-
pH 7.5, 20°C, mutant enzyme R165K/R277K
17
-
mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5
17
-
pH 7.5, 20°C, mutant enzyme R277G
19.2
-
pH 7.5, 20°C, mutant enzyme R277H
31.4
-
pH 7.5, 20°C, mutant enzyme R165G/R277K
47
-
pH 7.5, 20°C, mutant enzyme R277G
73
-
pH 7.5, 20°C, mutant enzyme R277L
0.3
-
recombinant mandelate racemase, putative misfolded form with N-terminal hexahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
0.6
-
mutant V29L, pH 7.5, 25°C
0.6
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29L
0.6
-
recombinant mrIII fusion protein bearing an N-terminal StrepII-tag and a C-terminal decahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
0.62
-
25°C, pH 7.5, wild-type enzyme
0.8
-
recombinant mandelate racemase represents correctly folded enzyme with N-terminal hexahistidine tag, in Na-HEPES buffer (0.1 M, pH 7.5),3.3 mM MgCl2
0.97
-
pH 7.5 at 25°C, 3.3 mM Mg2+, wild-type
0.97
-
wild-type, pH 7.5, 25°C
1
-
pH 7.5, 25°C, recombinant wild-type enzyme
1.07
-
pH 7.5 at 25°C, 20 mM Mg2+, wild-type
1.07
-
wild-type, pH 7.5, 25°C, presence of 20 mM Mg2+
1.1
-
mutant V26A/V29L, pH 7.5, 25°C
1.1
-
mutant V26F, pH 7.5, 25°C
1.1
-
mutant V26L, pH 7.5, 25°C
1.1
-
mutant V29F, pH 7.5, 25°C
1.1
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L
1.1
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26F
1.1
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26L
1.1
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29F
1.1
-
recombinant mandelate racemase, replacement of the N-terminal hexahistidine tag by a StrepII-tag appears to ameliorate the folding problem yielding a single enzyme species, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2
1.4
-
25°C, pH 7.5, mutant enzyme N197A
1.5
-
mutant V22I/V29L, pH 7.5, 25°C, presence of 20 mM Mg2+
1.5
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A/V29L
1.7
-
mutant V22I, pH 7.5, 25°C, presence of 20 mM Mg2+
1.7
-
mutant V26A, pH 7.5, 25°C
1.7
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22I
1.7
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V26A
1.8
-
mutant A25V, pH 7.5, 25°C
1.8
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant A25V
3
-
mutant T24S, pH 7.5, 25°C
3
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant T24S
3.4
-
mutant V22A, pH 7.5, 25°C
3.4
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22A
3.8
-
mutant enzyme F52W/Y64W
3.9
-
mutant V29A, pH 7.5, 25°C
3.9
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V29A
6.1
-
mutant V22F, pH 7.5, 25°C
6.1
-
pH 7.5 at 25°C, 3.3 mM Mg2+, mutant V22F
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Mandelate racemase and muconate lactonizing enzyme are mechanistically distinct and structurally homologous
1990
Neidhart, D.J.; Kenyon, G.L.; Gerlt, J.A.; Petsko, G.A.
Nature
347
692-694
Kinetics and mechanism of benzoylformate decarboxylase using 13C and solvent deuterium isotope effects on benzoylformate and benzoylformate analogues
1988
Weiss, P.M.; Garcia, G.A.; Kenyon, G.L.; Cleland, W.W.; Cook, P.F.
Biochemistry
27
2197-2205
Mandelate pathway of Pseudomonas putida: sequence relationships involving mandelate racemase, (S)-mandelate dehydrogenase, and benzoylformate decarboxylase and expression of benzoylformate decarboxylase in Escherichia coli
1990
Tsou, A.Y.; Ransom, S.C.; Gerlt, J.A.; Buechter, D.D.; Babbitt, P.C.; Kenyon, G.L.
Biochemistry
29
9856-9862
Preliminary X-ray data on crystals of mandelate racemase
1988
Neidhart, D.J.; Powers, V.M.; Kenyon, G.L.; Tsou, A.Y.; Ransom, S.C.; Gerlt, J.A.; Petsko, G.A.
J. Biol. Chem.
263
9268-9270
Cloning, DNA sequence analysis, and expression in Escherichia coli of the gene for mandelate racemase from Pseudomonas putida
1988
Ransom, S.C.; Gerlt, J.A.; Powers, V.M.; Kenyon, G.L.
Biochemistry
27
540-545
-
Evidence for the generation of alpha-carboxy-alpha-hydroxy-p-xylylene from p-(bromomethyl)mandelate by mandelate racemase
1988
Lin, D.T.; Powers, V.M.; Reynolds, L.J.; Whitman, C.P.; Kozarich, J.W.; Kenyon, G.L.
J. Am. Chem. Soc.
110
323-324
Symmetry and asymmetry in mandelate racemase catalysis
1985
Whitman, C.P.; Hegeman, G.D.; Cleland, W.W.; Kenyon, G.L.
Biochemistry
24
3936-3942
Mandelate racemase
1979
Kenyon, G.L.; Hegeman, G.D.
Adv. Enzymol. Relat. Areas Mol. Biol.
50
325-360
Mandelate racemase
1977
Kenyon, G.L.; Hegeman, G.D.
Methods Enzymol.
46
541-548
Mandelate racemase from Pseudomonas putida. Magnetic resonance and kinetic studies of the mechanism of catalysis
1975
Maggio, E.T.; Kenyon, G.L.; Mildvan, A.S.; Hegeman, G.D.
Biochemistry
14
1131-1139
Mandelate racemase from Pseudomonas putida. Affinity labeling of the enzyme by D,L-alpha-phenylglycidate in the presence of magnesium ion
1974
Fee, J.A.; Hegeman, G.D.; Kenyon, G.L.
Biochemistry
13
2533-2538
Mandelate racemase from pseudomonas putida. Subunit composition and absolute divalent metal ion requirement
1974
Fee, J.A.; Hegeman, G.D.; Kenyon, G.L.
Biochemistry
13
2528-2532
-
Mandelate racemase (Pseudomonas putida)
1970
Hegeman, G.D.
Methods Enzymol.
17
670-674
Mandelic acid racemase from Pseudomonas putida. Purification and properties of the enzyme
1970
Hegeman, G.D.; Rosenberg, E.Y.; Kenyon, G.L.
Biochemistry
9
4029-4036
Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the D270N mutant
1996
Schafer, S.L.; Barrett, W.C.; Kallarakal, A.T.; Mitra, B.; Kozarich, J.W.; Gerlt, J.A.
Biochemistry
35
5662-5669
A direct kinetic assay for mandelate racemase using circular dichroic measurements
1979
Sharp, T.R.; Hegeman, G.D.; Kenyon, G.L.
Anal. Biochem.
94
329-334
Mandelate racemase from Pseudomonas putida. Absence of detectable intermolecular proton transfer accompanying racemization
1977
Sharp, T.R.; Hegeman, G.D.; Kenyon, G.L.
Biochemistry
16
1123-1128
Mandelic acid racemase from Pseudomonas putida. Evidence favoring a carbanion intermediate in the mechanism of action
1970
Kenyon, G.L.; Hegeman, G.D.
Biochemistry
9
4036-4043
Selection and characterization of a mutant of the cloned gene for mandelate racemase that confers resistance to an affinity label by greatly enhanced production of enzyme
1989
Tsou, A.Y.; Ransom, S.C.; Gerlt, J.A.; Powers, V.M.; Kenyon, G.L.
Biochemistry
28
969-975
Restructuring catalysis in the mandelate pathway
1990
Neidhart, D.C.; Howell, P.L.; Petsko, G.A.; Gerlt, J.A.; Kozarich, J.W.; Powers, V.M.; Kenyon, G.L.
Biochem. Soc. Symp.
57
135-141
Mechanism of the reaction catalyzed by mandelate racemase. 3. Asymmetry in reactions catalyzed by the H297N mutant
1991
Landro, J.A.; Kallarakal, A.T.; Ransom, S.C.; Gerlt, J.A.; Kozarich, J.W.; Neidhart, D.J.; Kenyon, G.L.
Biochemistry
30
9274-9281
Mechanism of the reaction catalyzed by mandelate racemase. 2. Crystal structure of mandelate racemase at 2.5-A resolution: identification of the active site and possible catalytic residues
1991
Neidhart, D.J.; Howell, P.L.; Petsko, G.A.; Powers, V.M.; Li, R.; Kenyon, G.L.; Gerlt, J.A.
Biochemistry
30
9264-9273
Mechanism of the reaction catalyzed by mandelate racemase. 1. Chemical and kinetic evidence for a two-base mechanism
1991
Powers, V.M.; Koo, C.W.; Kenyon, G.L.; Gerlt, J.A.; Kozarich, J.W.
Biochemistry
30
9255-9263
-
Mandelate racemase and class-related enzymes
1992
Gerlt, J.A.; Kenyon, G.L.; Kozarich, J.W.; Neidhart, D.J.; Petsko, G.A.; Powers, V.M.
Curr. Opin. Struct. Biol.
2
736-742
The role of lysine 166 in the mechanism of mandelate racemase from Pseudomonas putida: mechanistic and crystallographic evidence for stereospecific alkylation by (R)-alpha-phenylglycidate
1994
Landro, J.A.; Gerlt, J.A.; Kozarich, J.W.; Koo, C.W.; Shah, V.J.; Kenyon, G.L.; Neidhart, D.J.; Fujita, S.; Petsko, G.A.
Biochemistry
33
635-643
-
Racemization of vinylglycolate catalyzed by mandelate racemase
1995
Li, R.; Powers, V.M.; Kozarich, J.W.; Kenyon, G.L.
J. Org. Chem.
60
3347-3351
Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant
1995
Kallarakal, A.T.; Mitra, B.; Kozarich, J.W.; Gerlt, J.A.; Clifton, J.G.; Petsko, G.A.; Kenyon, G.L.
Biochemistry
34
2788-2797
-
Large-scale production of mandelate racemase by Pseudomonas putida ATCC 12633: optimization of enzyme induction and development of a stable crude enzyme preparation
1997
Stecher, H.; Felfer, U.; Faber, K.
J. Biotechnol.
56
33-40
Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317
1995
Mitra, B.; Kallarakal, A.T.; Kozarich, J.W.; Gerlt, J.A.; Clifton, J.G.; Petsko, G.A.; Kenyon, G.L.
Biochemistry
34
2777-2787
Reaction intermediate analogues for mandelate racemase: interaction between Asn 197 and the alpha-hydroxyl of the substrate promotes catalysis
2000
ST.Maurice, M.; Bearne, S.L.
Biochemistry
39
13324-13335
Involvement of 4-hydroxymandelic acid in the degradation of mandelic acid by Pseudomonas convexa
1976
Bhat, S.G.; Vaidyanathan, C.S.
J. Bacteriol.
127
1108-1118
Production of R-(-)-mandelic acid from mandelonitrile by Alcaligenes faecalis ATCC 8750
1991
Yamamoto, K.; Oishi, K.; Fujimatsu, I.; Komatsu, K.
Appl. Environ. Microbiol.
57
3028-3032
-
Mandelamide hydrolase from Pseudomonas putida
1997
Kooo, C.W.
Diss. Abstr. Int. B
58
1865
Re-design of Saccharomyces cerevisiae flavocytochrome b2: introduction of L-mandelate dehydrogenase activity
1998
Sinclair, R.; Reid, G.A.; Chapman, S.K.
Biochem. J.
333
117-120
Kinetic and crystallographic studies on the active site Arg289Lys mutant of flavocytochrome b2 (yeast L-lactate dehydrogenase)
2000
Mowat, C.G.; Beaudoin, I.; Durley, R.C.; Barton, J.D.; Pike, A.D.; Chen, Z.W.; Reid, G.A.; Chapman, S.K.; Mathews, F.S.; Lederer, F.
Biochemistry
39
3266-3275
The catalytic role of tyrosine 254 in flavocytochrome b2 (L-lactate dehydrogenase from baker's yeast). Comparison between the Y254F and Y254L mutant proteins
2001
Gondry, M.; Duboist, J.; Terrier, M.; Lederer, F.
Eur. J. Biochem.
268
4918-4927
The role of a beta barrel loop 4 extension in modulating the physical and functional properties of long-chain 2-hydroxy-acid oxidase isozymes
1996
Belmouden, A.; Lederer, F.
Eur. J. Biochem.
238
790-798
Rat kidney L-2-hydroxyacid oxidase. Structural and mechanistic comparison with flavocytochrome b2 from bakerÆs yeast
1988
Urban, P.; Chirat, I.; Lederer, F.
Biochemistry
27
7365-7371
Crystalline mammalian L-amino acid oxidase from rat kidney mitochondria
1966
Nakano, M.; Danowski, T.S.
J. Biol. Chem.
241
2075-2083
Studies on L-amino-acid oxidase. I. Effects of pH and competitive inhibitors
1968
De Kok, A.; Veeger, C.
Biochim. Biophys. Acta
167
35-47
Non-linear slow-binding inhibition of Aerococcus viridans lactate oxidase by Cibacron Blue 3GA
2001
Streitenberger, S.A.; Lopez-Mas, J.A.; Sanchez-Ferrer, A.; Garcia-Carmona, F.
J. Enzyme Inhib.
16
301-312
On the reaction mechanism of L-lactate oxidase: quantitative structure-activity analysis of the reaction with para-substituted L-mandelates
1997
Yorita, K.; Janko, K.; Aki, K.; Ghisla, S.; Palfey, B.A.; Massey, V.
Proc. Natl. Acad. Sci. USA
94
9590-9595
Conversion of L-lactate oxidase to a long chain alpha-hydroxyacid oxidase by site-directed mutagenesis of alanine 95 to glycine
1996
Yorita, K.; Aki, K.; Ohkuma-Soyejima, T.; Kokubo, T.; Misaki, H.; Massey, V.
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271
28300-28305
Mandelic acid-4-hydroxylase, a new inducible enzyme from Pseudomonas convexa
1973
Bhat, S.G.; Ramanarayanan, M.; Vaidyanathan, C.S.
Biochem. Biophys. Res. Commun.
52
834-842
Purifications and properties of L-mandelate-4-hydroxylase from Pseudomonas convexa
1976
Bhat, S.G.; Vaidyanathan, C.S.
Arch. Biochem. Biophys.
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