1.1.1.B20: meso-2,3-butandiol dehydrogenase
This is an abbreviated version!
For detailed information about meso-2,3-butandiol dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.B20
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1.1.1.B20
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klebsiella
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diacetyl
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pneumoniae
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fed-batch
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nadh-dependent
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2s,3s-2,3-butanediol
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enterobacter
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synthesis
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serratia
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marcescens
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cloacae
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hydrolysate
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acetobacter
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biofuels
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polymyxa
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lactis
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byproduct
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acetolactate
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1,4-butanediol
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bioconversion
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aerogenes
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racemic
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refolding
- 1.1.1.B20
-
klebsiella
- diacetyl
- pneumoniae
-
fed-batch
-
nadh-dependent
-
2s,3s-2,3-butanediol
-
enterobacter
- synthesis
-
serratia
- marcescens
- cloacae
- hydrolysate
-
acetobacter
-
biofuels
- polymyxa
- lactis
-
byproduct
- acetolactate
- 1,4-butanediol
-
bioconversion
- aerogenes
-
racemic
-
refolding
Reaction
Synonyms
(2R,3R)-2,3-butanediol dehydrogenase, 2,3-BD dehydrogenase, 2,3-butanediol dehydrogenase, 2,3-butanediol dehydrogenases, ADH-9, ARA1, BDH, BdhA, BS-BDH, BtBDH, budC, butACg, butanediol dehydrogenase, ButB, CG-BDH, Cgl2674, mbdh, meso-2,3-BD dehydrogenase, meso-2,3-BDH, meso-2,3-butanediol dehydrogenase, meso-acetoin reductase, meso-BD, meso-BDH, MF996569, More, NAD(H)-dependent meso-2,3-BDH, NAD(H)-dependent meso-2,3-butanediol dehydrogenase, PA4153, PB24_3312, PF-BDH, PF1960, PT-BDH, R,R-2,3-butanediol dehydrogenase/meso-2,3-butanediol dehydrogenase/diacetyl reductase, SmBdh
ECTree
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Crystallization
Crystallization on EC 1.1.1.B20 - meso-2,3-butandiol dehydrogenase
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in complex with substrate meso-2,3-butanediol and inhibitor 2-mercaptoethanol, to 1.7 A resolution. The overall structure is similar to that of other short chain dehydrogenase/reductase enzymes, the NAD+ binding site, and the positions of catalytic residues Ser139, Tyr152, and Lys156 are also conserved. 2-Mercaptoethanol forms hydrogens bonds with residues Gln 140 and Gly 183 close to the active site, which are important but not sufficient for distiguishing stereoisomerism of a chiral substrate
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recombinant wild-type and mutant SmBdh proteins in complex with NAD+ and acetoin both bound in the active site, sitting drop vapor diffusion method, protein solution for wild-type SmBdh contains 9 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 200 mM acetoin, the protein solution for mutant SmBdh Q247A consists of 4.2 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 20 mM acetoin, and for mutant SmBdh Q247V/V139Q of 14.5 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 20 mM acetoin, the well solution contains 0.1 M sodium malonate, pH 6-7 and 6-15% w/v PEG 3350, mixing of 200 nl of protein with 100-300 nl of well solution, equilibration against 0.05 ml of well solution, 20°C, X-ray diffraction structure determination and analysis at 1.8-2.0 A resolution
recombinant wild-type and mutant SmBdh proteins in complex with with NAD+ and acetoin both bound in the active site, sitting drop vapor diffusion method, protein solution for wild-type SmBdh contains 9 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 200 mM acetoin, the protein solution for mutant SmBdh Q247A consists of 4.2 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 20 mM acetoin, and for mutant SmBdh Q247V/V139Q of 14.5 mg/ml of protein, 20 mM Tris, pH 7.5, 100 mM NaCl, 20 mM NAD+, and 20 mM acetoin, the well solution contains 0.1 M sodium malonate, pH 6-7 and 6-15% w/v PEG 3350, mixing of 200 nl of protein with 100-300 nl of well solution, equilibration against 0.05 ml of well solution, 20°C, X-ray diffraction structure determination and analysis at 1.8-2.0 A resolution