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.

Reaction

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

Synonyms

(2R,3R)-2,3-butanediol dehydrogenase, (R)-2,3-butanediol dehydrogenase, (R)-diacetyl reductase, 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, ADH-9, aminopropanol oxidoreductase, AR/BDH, BDH, BDH1, BDH99::67, BdhA, ButA, 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, NAD(H)-dependent 2,3-butanediol dehydrogenase, NADH-dependent 2,3-butanediol dehydrogenase, R,R-BD-DH, R,R-BDH, 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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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