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1.1.1.4: (R,R)-butanediol dehydrogenase

This is an abbreviated version!
For detailed information about (R,R)-butanediol dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.4

Reaction

(R,R)-butane-2,3-diol
+
NAD+
=
(R)-acetoin
+
NADH
+
H+

Synonyms

(2R,3R)-2,3-BDH, (2R,3R)-2,3-butanediol dehydrogenase, (R)-2,3-butanediol dehydrogenase, (R)-diacetyl reductase, (R,R)-butane-2,3-diol dehydrogenase, 1-amino-2-propanol dehydrogenase, 1-amino-2-propanol oxidoreductase, 2,3-BDH/AR, 2,3-butanediol dehydrogenase, 2,3-butanediol dehydrogenase/acetoin reductase, 2R,3R-2,3-BD dehydrogenase, 2R-3R-BDH, acetoin reductase, acetoin/diacetyl reductase, ADH-9, aminopropanol oxidoreductase, AR/BDH, BaBdhA, BcBDH, BDH, BDH1, Bdh1p, BDH2, Bdh2p, BDH99::67, BdhA, BtBDH, ButA, butanediol dehydrogenase, ButB, butylene glycol dehydrogenase, butyleneglycol dehydrogenase, D-(-)-butanediol dehydrogenase, D-1-amino-2-propanol dehydrogenase, D-1-amino-2-propanol:NAD+ oxidoreductase, D-2,3-BD dehydrogenase, D-aminopropanol dehydrogenase, dehydrogenase, D-aminopropanol, dehydrogenase, D-butanediol, DHAD, diacetyl reductase (acetoin), EC 1.1.1.74, GDH, GldA, meso-2,3-butanediol dehydrogenase, meso-BDH, MF996569, More, NAD(H)-dependent 2,3-butanediol dehydrogenase, NADH-dependent 2,3-butanediol dehydrogenase, PA4153, PB24_3312, R,R-2,3-butanediol dehydrogenase/meso-2,3-butanediol dehydrogenase/diacetyl reductase, R,R-BD-DH, R,R-BDH, R-selective 2,3-butanediol dehydrogenase, SLAC

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.4 (R,R)-butanediol dehydrogenase

Engineering

Engineering on EC 1.1.1.4 - (R,R)-butanediol dehydrogenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D194G
G198D/S199 V/P201E/Y218A
mutant displays no detectable activity with NADPH as cofactor, but uses NADH with kcat/Km value of 12 per s and mM
S199A
increase in catalytic efficiencies
S199C
decrease in catalytic efficiencies, with no significant changes in substrate preference
S199G
decrease in catalytic efficiencies, with no significant changes in substrate preference
S199R
increase in catalytic efficiencies
S199W
decrease in catalytic efficiencies, with no significant changes in substrate preference
E221S the
mutation produces a 170fold decrease in the Vm/Km with NADH because of a simultaneous 16fold increase in the Km value and an 11fold decrease in the Vm value, the mutation provides a positive effect on NADPH coenzyme specificity
E221S/I222R
mutant with preference for NADPH as coenzyme
E221S/I222R/A223S
mutant with preference for NADPH as coenzyme
additional information