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

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
1.1.1.4
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RECOMMENDED NAME
GeneOntology No.
(R,R)-butanediol dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R,R)-butane-2,3-diol + NAD+ = (R)-acetoin + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
(R,R)-butanediol biosynthesis
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(R,R)-butanediol degradation
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acetoin degradation
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Butanoate metabolism
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SYSTEMATIC NAME
IUBMB Comments
(R,R)-butane-2,3-diol:NAD+ oxidoreductase
Also converts diacetyl into acetoin with NADH as reductant.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-09-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
authors suggest systematic name: -glycol:NAD+ oxidoreductase ???
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain Ov 421, isolated from ovine milk
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Manually annotated by BRENDA team
strain Ov 421, isolated from ovine milk
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Manually annotated by BRENDA team
strain ET C9, isolated from artisanal goat's milk cheese
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Manually annotated by BRENDA team
strain ET C9, isolated from artisanal goat's milk cheese
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Manually annotated by BRENDA team
strain ME-303
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Manually annotated by BRENDA team
strain ME-303
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Manually annotated by BRENDA team
2,3-butanediol dehydrogenase 1 and 2; subsp. lactis D10
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
gene mbd1
UniProt
Manually annotated by BRENDA team
gene mbd1
UniProt
Manually annotated by BRENDA team
isolated from soil
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
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deletion of BDH1 results in an accumulation of acetoin and a diminution of 2,3-butanediol in two Saccharomyces cerevisiae strains under two different growth conditions
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R,3R)-2,3-butanediol + NAD+
(3R)-acetoin + NADH
show the reaction diagram
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
show the reaction diagram
(3R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
show the reaction diagram
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?
(3R,3S)-acetoin + NADH
(2R,3R)-2,3-butanediol + meso-2,3-butanediol + NAD+
show the reaction diagram
(3S)-acetoin + NADH + H+
(2R,3S)-butane-2,3-diol + NAD+
show the reaction diagram
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-
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?
(R)-1,2-propanediol + NAD+
hydroxyacetone + NADH + H+
show the reaction diagram
73% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction, very low activity with the (S)-enantiomer
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?
(R)-acetoin + NADH + H+
(2R,3R)-butane-2,3-diol + NAD+
show the reaction diagram
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?
(R)-acetoin + NADPH + H+
(2R,3R)-butane-2,3-diol + NADP+
show the reaction diagram
wild type enzyme does not use NADPH as coenzyme
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?
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
show the reaction diagram
(R,S)-3-hydroxy-2-pentanone + NADH
2,3-pentanediol + NAD+
show the reaction diagram
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r
(R,S)-4-hydroxy-3-pentanone + NADH
2,3-pentanediol + NAD+
show the reaction diagram
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r
1,2-butanediol + NAD+
?
show the reaction diagram
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?
1,2-hexanediol + NAD+
? + NADH + H+
show the reaction diagram
50% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction
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?
1,2-pentandiol + NAD+
? + NADH + H+
show the reaction diagram
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-
r
1,2-pentanediol + NAD+
? + NADH + H+
show the reaction diagram
74% activity compared to (2R,3R)-butane-2,3-diol in the oxidation reaction
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?
1,2-propandiol + NAD+
? + NADH + H+
show the reaction diagram
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r
1,2-propanediol + NAD+
?
show the reaction diagram
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?
1-hydroxy-2-butanone + NADH
?
show the reaction diagram
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?
1-hydroxy-2-propanone + NADH + H+
propane-1,2-diol + NAD+
show the reaction diagram
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r
2,3-butanediol + NAD+
acetoin + NADH
show the reaction diagram
2,3-butanediol + NAD+
acetoin + NADH + H+
show the reaction diagram
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r
2,3-pentanediol + NAD+
4-hydroxy-3-pentanone + 3-hydroxy-2-pentanone + NADH
show the reaction diagram
2-pentanone + NADH
(S)-2-pentanol + NAD+
show the reaction diagram
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?
2-propanol + NAD+
2-propanone + NADH + H+
show the reaction diagram
acetoin + NAD+
diacetyl + NADH
show the reaction diagram
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18% of the activity with 2,3-butanediol, in the reverse reaction 150% of the activity with acetoin
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r
acetoin + NADH
2,3-butanediol + NAD+
show the reaction diagram
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r
acetoin + NADH + H+
2,3-butanediol + NAD+
show the reaction diagram
cyclohexanone + NADH
?
show the reaction diagram
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38% of the activity with acetoin
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?
diacetyl + NADH
2,3-butanediol + NAD+
show the reaction diagram
diacetyl + NADH + H+
acetoin + NAD+
show the reaction diagram
dihydroxyacetone + NADH
?
show the reaction diagram
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36% of the activity with acetoin
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?
dihydroxyacetone phosphate + NADH
?
show the reaction diagram
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82% of the activity with acetoin
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?
ethyl pyruvate + NADH
?
show the reaction diagram
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?
glycerol + NAD+
? + NADH + H+
show the reaction diagram
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r
hydroxyacetone + NADH
1,2-propanediol
show the reaction diagram
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?
meso-2,3-butanediol + NAD+
D-(-)-acetoin + NADH
show the reaction diagram
meso-butane-2,3-diol + NAD+
acetoin + NADH + H+
show the reaction diagram
methyl glyoxal + NADH
?
show the reaction diagram
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?
methyl pyruvate + NADH
?
show the reaction diagram
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?
pyruvic aldehyde + NADH
?
show the reaction diagram
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81% of the activity with acetoin
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?
rac-1,2-propanediol + NAD+
hydroxyacetone + NADH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2R,3R)-butane-2,3-diol + NAD+
(3R,3S)-acetoin + NADH + H+
show the reaction diagram
(R,R)-butane-2,3-diol + NAD+
(R)-acetoin + NADH + H+
show the reaction diagram
rac-1,2-propanediol + NAD+
hydroxyacetone + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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14% of the activity with NAD+
additional information
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no activity with NADP+ or NADPH as the coenzyme, respectively
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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activation
Mn2+
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activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-Methylpyrazole
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5,5'-dithiobis(2-nitrobenzoic acid)
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Borate buffer
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dipicolinate
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NADH
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NADH availability limits the 2,3-butanediol dehydrogenase reaction
o-phenanthroline
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14
(2R,3R)-2,3-butanediol
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1.76 - 7.67
(2R,3R)-butane-2,3-diol
0.06 - 4.5
(3R,3S)-acetoin
3 - 161
(R)-acetoin
38
1,2-propanediol
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14.5
1-hydroxy-2-propanone
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2.6 - 86.8
2,3-Butanediol
6
2,3-pentanediol
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0.4 - 6.5
acetoin
3.3
D-(-)2,3-butanediol
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1.6 - 87
diacetyl
20
ethyl pyruvate
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6.25
meso-2,3-butanediol
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2.73 - 5.62
meso-butane-2,3-diol
75
methyl glyoxal
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18
Methyl pyruvate
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0.16 - 2.3
NAD+
0.045 - 0.7
NADH
0.044 - 0.087
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1
wild type enzyme, using 1 mM NADPH as cosubstrate
4.1
mutant enzyme E221S, using 1 mM NADH as cosubstrate
4.65
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purified native enzyme, pH 7.0, 30C
4.8
mutant enzyme E221S/I222R, using 1 mM NADH as cosubstrate
5.1
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acetoin, enzyme 1
6.1
mutant enzyme E221S/I222R/A223S, using 1 mM NADH as cosubstrate
7.55
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acetoin, enzyme 2
13.7
mutant enzyme E221S, using 1 mM NADPH as cosubstrate
35.55
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diacetyl, enzyme 2
35.6
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diacetyl, enzyme 1
54.7
mutant enzyme E221S/I222R, using 1 mM NADPH as cosubstrate
92
wild type enzyme, using 1 mM NADH as cosubstrate
93.2
mutant enzyme E221S/I222R/A223S, using 1 mM NADPH as cosubstrate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
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substrate reduction, enzyme 1
6
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oxidation reaction
6.7
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substrate reduction
7
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acetoin reduction
7.2
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substrate oxidation
7.5
assay at, oxidation reaction
8.5
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substrate oxidation, enzyme 2
8.8
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oxidation of secondary alcohols
9
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D(-)-2,3-butanediol oxidation
11
oxidation reaction
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
60 - 62
100
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catalytic activity increases up to
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
isoelectric focussing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30000
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gel filtration
61000
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gel filtration
81800
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gel filtration
90000
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gel filtration
100000 - 107000
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gel filtration
140000
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gel filtration
170000
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enzyme 1 and 2, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 32000, SDS-PAGE
tetramer
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4 * 35000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8.5
stable, rapid denaturation below pH 5.0
721872
7 - 7.6
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246407
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
rapid denaturation of the purified enzyme above 50C
100
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half-life: 130 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
stable at -18C
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very sensitive to storage, even at -20C
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2,3-butanediol dehydrogenase 1 and 2; partially
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native enzyme 35fold to homogeneity by fractional ammonium sulfate precipitation, followed by two different steps of anion exchange chromatography
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native enzyme by anion exchange and hydrophobic interaction chromatography, followed by ultrafiltration and native PAGE
recombinant
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparison, subcloning in Escherichia coli strain JM109, expression in Escherichia coli strain BL21 (DE3)
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expression in Escherichia coli
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gene mbd1, DNA and amino acid sequence determination and analysis, phylogenetic analysis
open reading frame (ORF) scaffold99_orf00067, DNA and amino acid sequence determination and analysis, phylogenetic analysis
overexpression in Saccharomyces cerevisiae
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phylogenetic analysis
subcloning of mutant proteins via plasmids in Bacillus subtilis strain WN1038
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced upon glucose depletion
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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