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0.1
-
pH 7.0, 30°C, mutant enzyme L239M/T245A
0.2
-
pH 7.0, 30°C, mutant enzyme F236V
1.3
-
pH 7.0, 30°C, mutant enzyme T245A
9.5
-
pH 7.0, 30°C, mutant enzyme F236S
20
-
pH 7.0, 30°C, mutant enzyme L239F
22
-
pH 7.0, 30°C, mutant enzyme L239W
92
-
pH 7.0, 30°C, mutant enzyme G234V/G235D
150
-
pH 7.0, 30°C, mutant enzyme L239M
520
-
pH 7.0, 30°C, mutant enzyme L239A
18000
-
pH 7.0, 30°C, wild-type enzyme
0.833
-
pH 6.9, 85°C, under argon
1.33
-
pH 6.9, 85°C, under argon
0.06
-
mutant T45M, pH 9.5, 35°C
0.101
-
mutant E116V, pH 9.5, 35°C
0.182
-
wild-type, pH 9.5, 35°C
0.214
-
mutant T45M/E116V, pH 9.5, 35°C
1.2
-
mutant I472A/I476F, pH 6.5, 30°C
6.9
-
mutant I472A, pH 6.5, 30°C
0.07
-
pH 7.0, mutant enzyme H70A
0.46
-
mutant enzyme H70A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.46
-
pH and temperature not specified in the publication, mutant H70A
1.41
-
pH 7.0, mutant enzyme H281A
2
-
mutant enzyme H281T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
2.1
-
mutant enzyme H281A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
2.1
-
pH and temperature not specified in the publication, mutant H281A
4.45
-
pH 7.0, mutant enzyme S26A
4.5
-
mutant enzyme H70F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
4.5
-
pH and temperature not specified in the publication, mutant H70F
4.6
-
mutant enzyme I466A, at pH 6.0 and 30°C
5.1
-
wild type enzyme, at pH 6.0 and 30°C
5.6
-
mutant enzyme H70S, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
6.9
-
mutant enzyme H281Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
6.9
-
pH and temperature not specified in the publication, mutant H281Y
8.6
-
mutant enzyme H281Q, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
14
-
mutant enzyme H70L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
14
-
pH and temperature not specified in the publication, mutant H70L
15
-
mutant enzyme S26A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
15
-
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
15
-
pH and temperature not specified in the publication, mutant S26A
17
-
mutant enzyme H281W, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
19
-
mutant enzyme H281N in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
21
-
pH 6.0, 30°C, mutant enzyme A460I/F464I
26
-
mutant enzyme S26M, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
26
-
pH and temperature not specified in the publication, mutant S26M
42
-
mutant enzyme H70T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
62
-
pH 6.0, 30°C, mutant enzyme A460I
65
-
mutant enzyme H281F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
65
-
pH and temperature not specified in the publication, mutant H281F
94
-
mutant enzyme S26T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
123
-
pH 6.0, 30°C, mutant enzyme F464I
132
-
mutant enzyme S26L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
132
-
pH and temperature not specified in the publication, mutant S26L
222
-
wild type enzyme at pH 6.0 and 35°C
241
-
pH 7.0, wild-type enzyme
284
-
recombinant, his-tagged enzyme at pH 6.0 and 35°C
320
-
wild type enzyme, at pH 6.0 and 30°C
320
-
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
320
-
pH and temperature not specified in the publication, wild-type enzyme
426
-
at 30°C, in 50 mM potassium phosphate buffer, pH 6.5
1349
-
pH 6.0, 30°C, wild-type enzyme
0.01
-
mutant D29E, pH 6.5, 30°C
0.07
-
mutant E468D, pH 6.5, 30°C
0.29
-
mutant H115K, pH 6.5, 30°C
0.87
-
mutant E52D, pH 6.5, 30°C
2.25
-
mutant Q383T, pH 6.5, 30°C
11.6
-
wild-type, pH 6.5, 30°C
31.4
-
at pH 6.5, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
37.55
-
enzyme covalently immobilized to magnetic Fe3O4 nanoparticles via glutaraldehyde
0.26
-
pH 7.5, 30°C, D-mandelate dehydrogenase D-ManDH2
1.5
-
at pH 7.0 and 37°C
0.466
-
pH 6.9, 85°C, under argon
0.6
-
pH 6.9, 85°C, under argon
0.75
-
mutant E116V, pH 9.5, 35°C
1.12
-
mutant T45M/E116V, pH 9.5, 35°C
1.99
-
mutant T45M, pH 9.5, 35°C
9.38
-
wild-type, pH 9.5, 35°C
1.8
-
mutant I472A, pH 6.5, 30°C
4.4
-
mutant I472A/I476F, pH 6.5, 30°C
0.06
-
mutant enzyme L461V, in potassium phosphate buffer (pH 6.5, 50 mM)
0.2
-
mutant enzyme A460I
0.2
-
pH 6.0, 30°C, mutant enzyme A460I
0.23
-
in 50 mM potassium phosphate buffer, pH 6.5, at 30°C
0.25
-
mutant enzyme L461A, in potassium phosphate buffer (pH 6.5, 50 mM)
0.27
-
wild type enzyme, at pH 6.0 and 30°C
0.27
-
wild type enzyme, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.27
-
pH and temperature not specified in the publication, wild-type enzyme
0.29
-
mutant enzyme H281Q, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.29
-
mutant enzyme H281W, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.37
-
pH 7.0, wild-type enzyme
0.37
-
wild type enzyme, in potassium phosphate buffer (pH 6.5, 50 mM)
0.38
-
mutant enzyme H70L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.38
-
pH and temperature not specified in the publication, mutant H70L
0.4
-
mutant enzyme H281A
0.44
-
recombinant, his-tagged enzyme at pH 6.0 and 35°C
0.45
-
mutant enzyme T377L/A460Y, at pH 6.0 and 30°C
0.49
-
mutant enzyme H281Y, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.49
-
pH and temperature not specified in the publication, mutant H281Y
0.51
-
mutant enzyme P24A, in potassium phosphate buffer (pH 6.5, 50 mM)
0.54
-
mutant enzyme H281F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.54
-
wild type enzyme, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
0.54
-
pH and temperature not specified in the publication, mutant H281F
0.58
-
mutant enzyme L476Q
0.58
-
mutant enzyme L476Q, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
0.59
-
mutant enzyme L476G, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
0.6
-
mutant enzyme S181T/L476P, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
0.69
-
wild type enzyme at pH 6.0 and 35°C
0.8
-
mutant enzyme S26M, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.8
-
pH 6.0, 30°C, wild-type enzyme
0.8
-
pH and temperature not specified in the publication, mutant S26M
0.85
-
mutant enzyme H70F, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.85
-
mutant enzyme S26T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.85
-
pH and temperature not specified in the publication, mutant H70F
0.89
-
mutant enzyme H70T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.9
-
mutant enzyme H281T, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
0.94
-
mutant enzyme H70S, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1
-
mutant enzyme L476H, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.02
-
mutant enzyme L476T, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.03
-
mutant enzyme L476P, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.06
-
mutant enzyme L476Q/S525G, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.08
-
mutant enzyme L476M, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.1
-
mutant enzyme A460I/F464I
1.1
-
pH 6.0, 30°C, mutant enzyme A460I/F464I
1.14
-
mutant enzyme L476S, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.17
-
mutant enzyme L476A, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.2
-
mutant enzyme H281A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.2
-
mutant enzyme S26L, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.2
-
pH and temperature not specified in the publication, mutant H281A
1.2
-
pH and temperature not specified in the publication, mutant S26L
1.23
-
mutant enzyme S181T, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.26
-
mutant enzyme L476C, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.4
-
mutant enzyme L461G, in potassium phosphate buffer (pH 6.5, 50 mM)
1.46
-
mutant enzyme L476K, in 50 mM potassium phosphate buffer pH 7.0, 0.5 mM thiamine diphosphate, 2.5 mM MgSO4, at 30°C
1.5
-
mutant enzyme H70A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
1.5
-
pH and temperature not specified in the publication, mutant H70A
1.54
-
mutant enzyme A460G, in potassium phosphate buffer (pH 6.5, 50 mM)
1.68
-
pH 7.0, mutant enzyme H281A
1.92
-
pH 7.0, mutant enzyme H70A
2
3
wild type enzyme, at pH 6.0 and 30°C
2.3
-
mutant enzyme F464I
2.3
-
pH 6.0, 30°C, mutant enzyme F464I
2.9
-
mutant enzyme H281N in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
7.8
-
mutant enzyme S26A, in 100 mM potassium phosphate buffer (pH 6.0), at 30°C
7.8
-
pH and temperature not specified in the publication, mutant S26A
8.62
-
pH 7.0, mutant enzyme S26A
15
-
mutant enzyme I466A, at pH 6.0 and 30°C
7.5
-
in 50 mM potassium phosphate buffer, pH 6.8 in the presence of 2.5 mM MgSO4 and 0.1 mM thiamine diphosphate
0.024
-
mutant D29E, pH 6.5, 30°C
0.14
-
mutant E468D, pH 6.5, 30°C
0.27
-
mutant H115K, pH 6.5, 30°C
1.65
-
wild-type, pH 6.5, 30°C
1.71
-
mutant Q383T, pH 6.5, 30°C
2.72
-
mutant E52D, pH 6.5, 30°C
7.3
-
at pH 6.5, temperature not specified in the publication
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Anaerobic metabolism of L-phenylalanine via benzoyl-CoA in the denitrifying bacterium Thauera aromatica
1997
Schneider, S.; Mohamed, M.E.S.; Fuchs, G.
Arch. Microbiol.
168
310-320
L-Aspartate-beta-decarboxylase. Structure, catalytic activities, and allosteric regulation
1971
Tate, S.S.; Meister, A.
Adv. Enzymol. Relat. Areas Mol. Biol.
35
503-543
Differential reactivity in the processing of [p-(halomethyl)benzoyl]formates by benzoylformate decarboxylase, a thiamin pyrophosphate dependent enzyme
1988
Reynolds, L.J.; Garcia, G.A.; Kozarich, J.W.; Kenyon, G.L.
Biochemistry
27
5530-5538
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
-
Microbial metabolism of D- and L-phenylglycine by Pseudomonas putida LW-4
1986
Van den Tweel, W.J.J.; Smits, J.P.; de Bont, J.A.M.
Arch. Microbiol.
144
169-174
-
Inhibition of benzoylformate decarboxylase by [p-(bromomethyl)benzoyl]formate. Enzyme-catalyzed modification of thiamine pyrophosphate by halide elimination and tautomerization
1986
Dirmaier, L.J.; Garcia, G.A.; Kozarich, J.W.; Kenyon, G.L.
J. Am. Chem. Soc.
108
3149-3150
-
Immunological comparison of microbial TPP-dependent non-oxidative alpha-keto acid decarboxylase
1986
Barrowman, M.M.; Harnett, W.; Scott, A.J.; Fewson, C.A.; Kusel, J.R.
FEMS Microbiol. Lett.
34
57-60
Initial reactions involved in the dissimilation of mandelate by Rhodotorula graminis
1984
Durham, D.R.
J. Bacteriol.
160
778-780
Metabolism of mandelic acid by Neurospora crassa
1977
Ramakrishna Rao, D.N.; Vaidyanathan, C.S.
Can. J. Microbiol.
23
1496-1499
-
Negative Co-operativity in the benzoylformate decarboxylase of Acinetobacter calcoaceticus N.C.I.B. 8250
1973
Jamaluddin, M.; Fewson, C.A.
Biochem. Soc. Trans.
1
1258-1260
-
Benzoylformate decarboxylase (Pseudomonas putida)
1970
Hegeman, G.D.
Methods Enzymol.
17A
674-678
Application of alpha-keto acid decarbpoxylases in biotransformations
1998
Iding, H.; Siegert, P.; Mesch, K.; Pohl, M.
Biochim. Biophys. Acta
1385
307-322
The crystal structure of benzoylformate decarboxylase at 1.6 A resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes
1998
Hasson, M.S.; Muscate, A.; McLeish, M.J.; Polovnikova, L.S.; Gerlt, J.A.; Kenyon, G.L.; Petsko, G.A.; Ringe, D.
Biochemistry
37
9918-9930
Acyloin formation by benzoylformate decarboxylase from Pseudomonas putida
1992
Wilcocks, R.; Ward, O.P.; Collins, S.; Dewdney, N.J.; Hong, Y.; Prosen, E.
Appl. Environ. Microbiol.
58
1699-1704
Purification and crystallization of benzoylformate decarboxylase
1995
Hasson, M.S.; Muscate, A.; Henehan, G.T.M.; Guidinger, P.F.; Petsko, G.A.; Ringe, D.; Kenyon, G.L.
Protein Sci.
4
955-959
Isolation, characterization and mapping of mandelate pathway mutants of Acinetobacter calcoaceticus
1984
Vakeria, D.; Vivian, A.; Fewson, C.A.
J. Gen. Microbiol.
130
2893-2903
The effect of a non-metabolizable analog on mandelate catabolism in Pseudomonas putida
1976
Hegeman, G.D.; Root, R.
Arch. Microbiol.
110
19-25
Phenylglyoxylate:NAD+ oxidoreductase (CoA benzoylating), a new enzyme of anaerobic phenylalanine metabolism in the denitrifying bacterium Azoarcus evansii
1998
Hirsch, W.; Schägger, H.; Fuchs, G.
Eur. J. Biochem.
251
907-915
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
Highly efficient Aerococcus viridians L-alpha-glycerophosphate oxidase production in the presence of H2O2-decomposing agent: purification and kinetic characterization
2001
Streitenberger, S.A.; Lopez-Mas, J.A.; Sanchez-Ferrer, A.; Garcia-Carmona, J.A.
Appl. Microbiol. Biotechnol.
57
329-333
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
Crystalline mammalian L-amino acid oxidase from rat kidney mitochondria
1966
Nakano, M.; Danowski, T.S.
J. Biol. Chem.
241
2075-2083
L-alpha-Hydroxy acid oxidases of hog renal cortex
1962
Robinson, J.C.; Keay, L.; Molinari, R.; Sizer, I.W.
J. Biol. Chem.
237
2001-2010
Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874
1982
Lindstedt, S.; Rundgren, M.
J. Biol. Chem.
257
11922-11931
2-Keto acid oxidoreductases from Pyrococcus furiosus and Thermococcus litoralis
2001
Schut, G.J.; Menon, A.L.; Adams, M.W.W.
Methods Enzymol.
331
144-158
-
On a non-pyridine nucleotide-dependent 2-oxoacid reductase of broad specificity from two Proteus species
1985
Neumann, S.; Simon, H.
FEBS Lett.
167
29-32
Phenylacetyl-CoA:acceptor oxidoreductase, a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica
1999
Rhee, S.K.; Fuchs, G.
Eur. J. Biochem.
262
507-515
Phenylacetyl-CoA:acceptor oxidoreductase, a new a-oxidizing enzyme that produces phenylglyoxylate. Assay, membrane localization, and differential production in Thauera aromatica
1998
Schneider, S.; Fuchs, G.
Arch. Microbiol.
169
509-516
Characterization of 2-ketoisovalerate ferredoxin oxidoreductase, a new and reversible coenzyme A-dependent enzyme involved in peptide fermentation by hyperthermophilic archaea
1996
Heider, J.; Mai, X.; Adams, M.W.
J. Bacteriol.
178
780-787
Studies on structure-function relationships of indolepyruvate decarboxylase from Enterobacter cloacae, a key enzyme of the indole acetic acid pathway
2003
Schutz, A.; Golbik, R.; Tittmann, K.; Svergun, D.I.; Koch, M.H.; Hubner, G.; Konig, S.
Eur. J. Biochem.
270
2322-2331
Structural and kinetic analysis of catalysis by a thiamin diphosphate-dependent enzyme, benzoylformate decarboxylase
2003
Polovnikova, E.S.; McLeish, M.J.; Sergienko, E.A.; Burgner, J.T.; Anderson, N.L.; Bera, A.K.; Jordan, F.; Kenyon, G.L.; Hasson, M.S.
Biochemistry
42
1820-1830
Benzoylformate decarboxylase from Pseudomonas putida as stable catalyst for the synthesis of chiral 2-hydroxy ketones
2000
Iding, H.; Dünnwald, T.; Greiner, L.; Liese, A.; Müller, M.; et al.
Chem. Eur. J.
6
1483-1495
Alteration of the substrate specificity of benzoylformate decarboxylase from Pseudomonas putida by directed evolution
2003
Lingen, B.; Kolter-Jung, D.; Dunkelmann, P.; Feldmann, R.; Grotzinger, J.; Pohl, M.; Muller, M.
ChemBioChem
4
721-726
Intermediates and transition states in thiamin diphosphate-dependent decarboxylases. A kinetic and NMR study on wild-type indolepyruvate decarboxylase and variants using indolepyruvate, benzoylformate, and pyruvate as substrates
2005
Schutz, A.; Golbik, R.; Konig, S.; Hubner, G.; Tittmann, K.
Biochemistry
44
6164-6179
Exchanging the substrate specificities of pyruvate decarboxylase from Zymomonas mobilis and benzoylformate decarboxylase from Pseudomonas putida
2005
Siegert, P.; McLeish, M.J.; Baumann, M.; Iding, H.; Kneen, M.M.; Kenyon, G.L.; Pohl, M.
Protein Eng. Des. Sel.
18
345-357
High resolution structures of an oxidized and reduced flavoprotein. The water switch in a soluble form of (S)-mandelate dehydrogenase
2004
Sukumar, N.; Dewanti, A.R.; Mitra, B.; Mathews, F.S.
J. Biol. Chem.
279
3749-3757
-
Asymmetric synthesis of unnatural L-amino acids using thermophilic aromatic L-amino acid transaminase
2006
Cho, B.; Seo, J.; Kim, J.; Lee, C.; Kim, B.
Biotechnol. Bioprocess Eng.
11
299-305
-
Branched-chain keto acid decarboxylase from Lactococcus lactis (KdcA), a valuable thiamine diphosphate-dependent enzyme for asymmetric C-C bond formation
2007
Gocke, D.; Nguyen, C.L.; Pohl, M.; Stillger, T.; Walter, L.; Mueller, M.
Adv. Synth. Catal.
349
1425-1435
Identification of novel benzoylformate decarboxylases by growth selection
2006
Henning, H.; Leggewie, C.; Pohl, M.; Mueller, M.; Eggert, T.; Jaeger, K.E.
Appl. Environ. Microbiol.
72
7510-7517
Elucidation of the chemistry of enzyme-bound thiamin diphosphate prior to substrate binding: defining internal equilibria among tautomeric and ionization states
2007
Nemeria, N.; Korotchkina, L.; McLeish, M.J.; Kenyon, G.L.; Patel, M.S.; Jordan, F.
Biochemistry
46
10739-10744
Isolation and characterization of a benzoylformate decarboxylase and a NAD+/NADP+-dependent benzaldehyde dehydrogenase involved in D-phenylglycine metabolism in Pseudomonas stutzeri ST-201
2007
Saehuan, C.; Rojanarata, T.; Wiyakrutta, S.; McLeish, M.J.; Meevootisom, V.
Biochim. Biophys. Acta
1770
1585-1592
Protein-enhanced decarboxylation of the covalent intermediate in benzoylformate decarboxylase--Desolvation or acid catalysis?
2006
Kluger, R.; Yu, D.
Bioorg. Chem.
34
337-344
Factors mediating activity, selectivity, and substrate specificity for the thiamin diphosphate-dependent enzymes benzaldehyde lyase and benzoylformate decarboxylase
2006
Knoll, M.; Mueller, M.; Pleiss, J.; Pohl, M.
Chembiochem
7
1928-1934
An activity, stability and selectivity comparison of propioin synthesis by thiamine diphosphate-dependent enzymes in a solid/gas bioreactor
2007
Mikolajek, R.; Spiess, A.C.; Pohl, M.; Lamare, S.; Buechs, J.
Chembiochem
8
1063-1070
-
Asymmetric synthesis of aliphatic 2-hydroxy ketones by enzymatic carboligation of aldehydes
2007
Dominguez de Maria, P.; Pohl, M.; Gocke, D.; Groeger, H.; Trauthwein, H.; Stillger, T.; Walter, L.; Mueller, M.
Eur. J. Org. Chem.
2007
2940-2944
Accelerating unimolecular decarboxylation by preassociated acid catalysis in thiamin-derived intermediates: implicating Bronsted acids as carbanion traps in enzymes
2006
Kluger, R.; Ikeda, G.; Hu, Q.; Cao, P.; Drewry, J.
J. Am. Chem. Soc.
128
15856-15864
Mechanism-based inactivation of benzoylformate decarboxylase, a thiamin diphosphate-dependent enzyme
2007
Bera, A.K.; Polovnikova, L.S.; Roestamadji, J.; Widlanski, T.S.; Kenyon, G.L.; McLeish, M.J.; Hasson, M.S.
J. Am. Chem. Soc.
129
4120-4121
Feasibility of gas/solid carboligation: conversion of benzaldehyde to benzoin using thiamine diphosphate-dependent enzymes
2007
Mikolajek, R.; Spiess, A.C.; Buechs, J.
J. Biotechnol.
129
723-725
Improving the carboligase activity of benzoylformate decarboxylase from Pseudomonas putida by a combination of directed evolution and site-directed mutagenesis
2002
Lingen, B.; Grotzinger, J.; Kolter, D.; Kula, M.R.; Pohl, M.
Protein Eng.
15
585-593
Purification, characterization, gene cloning, and expression of a novel alcohol dehydrogenase with anti-prelog stereospecificity from Candida parapsilosis
2007
Nie, Y.; Xu, Y.; Mu, X.Q.; Wang, H.Y.; Yang, M.; Xiao, R.
Appl. Environ. Microbiol.
73
3759-3764
A new family of D-2-hydroxyacid dehydrogenases that comprises D-mandelate dehydrogenases and 2-ketopantoate reductases
2008
Wada, Y.; Iwai, S.; Tamura, Y.; Ando, T.; Shinoda, T.; Arai, K.; Taguchi, H.
Biosci. Biotechnol. Biochem.
72
1087-1094
Preparation and characterization of Saccharomyces cerevisiae alcohol dehydrogenase immobilized on magnetic nanoparticles
2008
Li, G.Y.; Huang, K.L.; Jiang, Y.R.; Yang, D.L.; Ding, P.
Int. J. Biol. Macromol.
42
405-412
Mechanism of benzaldehyde lyase studied via thiamin diphosphate-bound intermediates and kinetic isotope effects
2008
Chakraborty, S.; Nemeria, N.; Yep, A.; McLeish, M.J.; Kenyon, G.L.; Jordan, F.
Biochemistry
47
3800-3809
Detection and time course of formation of major thiamin diphosphate-bound covalent intermediates derived from a chromophoric substrate analogue on benzoylformate decarboxylase
2009
Chakraborty, S.; Nemeria, N.S.; Balakrishnan, A.; Brandt, G.S.; Kneen, M.M.; Yep, A.; McLeish, M.J.; Kenyon, G.L.; Petsko, G.A.; Ringe, D.; Jordan, F.
Biochemistry
48
981-994
Rational protein design of ThDP-dependent enzymes-engineering stereoselectivity
2008
Gocke, D.; Walter, L.; Gauchenova, E.; Kolter, G.; Knoll, M.; Berthold, C.L.; Schneider, G.; Pleiss, J.; Mueller, M.; Pohl, M.
ChemBioChem
9
406-412
Amino acids allosterically regulate the thiamine diphosphate-dependent alpha-keto acid decarboxylase from Mycobacterium tuberculosis
2008
Werther, T.; Spinka, M.; Tittmann, K.; Schütz, A.; Golbik, R.; Mrestani-Klaus, C.; Hübner, G.; König, S.
J. Biol. Chem.
283
5344-5354
Saturation mutagenesis of putative catalytic residues of benzoylformate decarboxylase provides a challenge to the accepted mechanism
2008
Yep, A.; Kenyon, G.L.; McLeish, M.J.
Proc. Natl. Acad. Sci. USA
105
5733-5738
Structural and kinetic studies on native intermediates and an intermediate analogue in benzoylformate decarboxylase reveal a least motion mechanism with an unprecedented short-lived predecarboxylation intermediate
2009
Bruning, M.; Berheide, M.; Meyer, D.; Golbik, R.; Bartunik, H.; Liese, A.; Tittmann, K.
Biochemistry
48
3258-3268
Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition
2010
Brandt, G.S.; Kneen, M.M.; Petsko, G.A.; Ringe, D.; McLeish, M.J.
J. Am. Chem. Soc.
132
438-439
-
Comparative characterisation of thiamin diphosphate-dependent decarboxylases
2009
Gocke, D.; Graf, T.; Brosi, H.; Frindi-Wosch, I.; Walter, L.; Müller, M.; Pohl, M.
J. Mol. Catal. B
61
30-35
The D-2-hydroxyacid dehydrogenase incorrectly annotated PanE is the sole reduction system for branched-chain 2-keto acids in Lactococcus lactis
2009
Chambellon, E.; Rijnen, L.; Lorquet, F.; Gitton, C.; Van Hylckama Vlieg, J.; Wouters, J.; Yvon, M.
J. Bacteriol.
191
873-881
Cloning and characterization of indolepyruvate decarboxylase from Methylobacterium extorquens AM1
2010
Fedorov, D.N.; Doronina, N.V.; Trotsenko, Y.A.
Biochemistry (Moscow)
75
1435-1443
Understanding the mode of action of ThDP in benzoylformate decarboxylase
2010
Topal, K.; Atilgan, C.; Demir, A.; Aviyente, V.
Biopolymers
93
32-46
Immobilization and characterization of benzoylformate decarboxylase from Pseudomonas putida on spherical silica carrier
2011
Peper, S.; Kara, S.; Long, W.S.; Liese, A.; Niemeyer, B.
Bioprocess Biosyst. Eng.
34
671-680
Characterization of a thiamin diphosphate-dependent phenylpyruvate decarboxylase from Saccharomyces cerevisiae
2011
Kneen, M.; Stan, R.; Yep, A.; Tyler, R.; Saehuan, C.; McLeish, M.
FEBS J.
278
1842-1853
Influence of reaction conditions on the enantioselectivity of biocatalyzed C-C bond formations under high pressure conditions
2011
Kara, S.; Long, W.S.; Berheide, M.; Peper, S.; Niemeyer, B.; Liese, A.
J. Biotechnol.
152
87-92
Physiological relation between respiration activity and heterologous expression of selected benzoylformate decarboxylase variants in Escherichia coli
2010
Palmen, T.G.; Nieveler, J.; Froelich, B.; Treffenfeldt, W.; Pohl, M.; Buechs, J.
Microb. Cell Fact.
9
76
Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics
2000
Hubbard, B.K.; Thomas, M.G.; Walsh, C.T.
Chem. Biol.
7
931-942
Oxidative decarboxylation of mandelic acid derivative by recombinant Escherichia coli: a novel method of ethyl vanillin synthesis
2013
Pan, X.X.; Li, J.J.; Wang, M.G.; He, W.S.; Jia, C.S.; Zhang, X.M.; Feng, B.; Li, D.L.; Zeng, Z.
Biotechnol. Lett.
35
921-927
Using site-saturation mutagenesis to explore mechanism and substrate specificity in thiamin diphosphate-dependent enzymes
2013
Andrews, F.H.; McLeish, M.J.
FEBS J.
280
6395-6411
-
Covalent immobilization of benzoylformate decarboxylase from Pseudomonas putida on magnetic epoxy support and its carboligation reactivity
2014
Tural, B.; Tarhan, T.; Tural, S.
J. Mol. Catal. B
102
188-194
Modified substrate specificity of L-hydroxyisocaproate dehydrogenase derived from structure-based protein engineering
1997
Feil, I.K.; Hendle, J.; Schomburg, D.
Protein Eng.
10
255-262
Two forms of NAD-dependent D-mandelate dehydrogenase in Enterococcus faecalis IAM 10071
2002
Tamura, Y.; Ohkubo, A.; Iwai, S.; Wada, Y.; Shinoda, T.; Arai, K.; Mineki, S.; Iida, M.; Taguchi, H.
Appl. Environ. Microbiol.
68
947-951
-
Purification and characterization of D(-)-mandelate dehydrogenase from Rhodotorula graminis
1989
Baker, D.P.; Fewson, C.A.
Microbiology
135
2035-2044
Heterologous pathway for the production of L-phenylglycine from glucose by E. coli
2014
Liu, S.P.; Liu, R.X.; El-Rotail, A.A.; Ding, Z.Y.; Gu, Z.H.; Zhang, L.; Shi, G.Y.
J. Biotechnol.
186
91-97
-
Stereoselective synthesis of L-tert-leucine by a newly cloned leucine dehydrogenase from Exiguobacterium sibiricum
2014
Li, J.; Pan, J.; Zhang, J.; Xu, J.
J. Mol. Catal. B
105
11-17
-
Purification and characterization of a novel carbonyl reductase involved in oxidoreduction of aromatic beta-amino ketones/alcohols
2014
He, S.; Wang, Z.; Zou, Y.; Chen, S.; Xu, X.
Process Biochem.
49
1107-1112
Perturbation of the monomer-monomer interfaces of the benzoylformate decarboxylase tetramer
2014
Andrews, F.H.; Rogers, M.P.; Paul, L.N.; McLeish, M.J.
Biochemistry
53
4358-4367
The kinetic characterization and X-ray structure of a putative benzoylformate decarboxylase from M. smegmatis highlights the difficulties in the functional annotation of ThDP-dependent enzymes
2015
Andrews, F.H.; Horton, J.D.; Shin, D.; Yoon, H.J.; Logsdon, M.G.; Malik, A.M.; Rogers, M.P.; Kneen, M.M.; Suh, S.W.; McLeish, M.J.
Biochim. Biophys. Acta
1854
1001-1009
-
Mechanistic and structural insight to an evolved benzoylformate decarboxylase with enhanced pyruvate decarboxylase activity
2016
Andrews, F.; Wechsler, C.; Rogers, M.; Meyer, D.; Tittmann, K.; McLeish, M.
Catalysts
6
190
Reducing 3,4-dihydroxyphenylpyruvic acid to D-3,4-dihydroxyphenyllactic acid via a coenzyme nonspecific D-lactate dehydrogenase from Lactobacillus reuteri
2018
Wang, Y.; Bai, Y.; Fan, T.; Zheng, X.; Cai, Y.
J. Appl. Microbiol.
125
1739-1748
Directed modification of L-LcLDH1, an L-lactate dehydrogenase from Lactobacillus casei, to improve its specific activity and catalytic efficiency towards phenylpyruvic acid
2018
Li, J.F.; Li, X.Q.; Liu, Y.; Yuan, F.J.; Zhang, T.; Wu, M.C.; Zhang, J.R.
J. Biotechnol.
281
193-198
-
Understanding substrate specificity and enantioselectivity of carbonyl reductase from Candida parapsilosis ATCC 7330 (CpCR) Experimental and modeling studies
2018
Aggarwal, N.; Ananthathamula, R.; Karanam, V.; Doble, M.; Chadha, A.
Mol. Catal.
460
40-45
-
Identification of a L-Lactate dehydrogenase with 3,4-dihydroxyphenylpyruvic reduction activity for L-danshensu production
2018
Lu, H.; Bai, Y.; Fan, T.; Zhao, Y.; Zheng, X.; Cai, Y.
Process Biochem.
72
119-123
The ternary complex structure of D-mandelate dehydrogenase with NADH and anilino(oxo)acetate
2017
Furukawa, N.; Miyanaga, A.; Nakajima, M.; Taguchi, H.
Biochem. Biophys. Res. Commun.
486
665-670
Rational engineering of Bacillus cereus leucine dehydrogenase towards alpha-keto acid reduction for improving unnatural amino acid production
2019
Zhou, J.; Wang, Y.; Chen, J.; Xu, M.; Yang, T.; Zheng, J.; Zhang, X.; Rao, Z.
Biotechnol. J.
14
e1800253
-
Structure-guided engineering of meso-diaminopimelate dehydrogenase for enantioselective reductive amination of sterically bulky 2-keto acids
2018
Cheng, X.; Chen, X.; Feng, J.; Wu, Q.; Zhu, D.
Catal. Sci. Technol.
8
4994-5002
-
Identification and rational engineering of a high substrate-tolerant leucine dehydrogenase effective for the synthesis of L-tert-leucine
2021
Meng, X.; Yang, L.; Liu, Y.; Wang, H.; Shen, Y.; Wei, D.
ChemCatChem
13
3340-3349
Cloning and expression of a novel leucine dehydrogenase characterization and L-tert-leucine production
2020
Luo, W.; Zhu, J.; Zhao, Y.; Zhang, H.; Yang, X.; Liu, Y.; Rao, Z.; Yu, X.
Front. Bioeng. Biotechnol.
8
186
Expression of novel L-leucine dehydrogenase and high-level production of L-tert-leucine catalyzed by engineered Escherichia coli
2021
Jia, Y.Y.; Xie, Y.L.; Yang, L.L.; Shi, H.L.; Lu, Y.F.; Zhang, S.P.; Tang, C.D.; Yao, L.G.; Kan, Y.C.
Front. Bioeng. Biotechnol.
9
655522
Biosynthesis of phenylglyoxylic acid by LhDMDH, a novel D-mandelate dehydrogenase with high catalytic activity
2018
Tang, C.D.; Shi, H.L.; Xu, J.H.; Jiao, Z.J.; Liu, F.; Ding, P.J.; Shi, H.F.; Yao, L.G.; Kan, Y.C.
J. Agric. Food Chem.
66
2805-2811
Design, synthesis, and biological evaluation of substrate-competitive inhibitors of C-terminal binding protein (CtBP)
2016
Korwar, S.; Morris, B.; Parikh, H.; Coover, R.; Doughty, T.; Love, I.; Hilbert, B.; Royer, W.J.; Kellogg, G.; Grossman, S.; Ellis, K.
Bioorg. Med. Chem.
24
2707-2715