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Information on EC 1.1.1.383 - ketol-acid reductoisomerase [NAD(P)+] and Organism(s) Escherichia coli and UniProt Accession P05793

for references in articles please use BRENDA:EC1.1.1.383
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IUBMB Comments
The enzyme, characterized from the bacteria Hydrogenobaculum sp. and Syntrophomonas wolfei subsp. wolfei and from the archaea Metallosphaera sedula and Ignisphaera aggregans, can use both NADH and NADPH with similar efficiency [cf. EC 1.1.1.86, ketol-acid reductoisomerase (NADP+) and EC 1.1.1.382, ketol-acid reductoisomerase (NAD+)].
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This record set is specific for:
Escherichia coli
UNIPROT: P05793
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
ilvC, Shewana3_0355, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
(2R)-2,3-dihydroxy-3-methylbutanoate:NAD(P)+ oxidoreductase (isomerizing)
The enzyme, characterized from the bacteria Hydrogenobaculum sp. and Syntrophomonas wolfei subsp. wolfei and from the archaea Metallosphaera sedula and Ignisphaera aggregans, can use both NADH and NADPH with similar efficiency [cf. EC 1.1.1.86, ketol-acid reductoisomerase (NADP+) and EC 1.1.1.382, ketol-acid reductoisomerase (NAD+)].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(S)-2-acetolactate + NADH + H+
2,3-dihydroxy-3-methylbutanoate + NAD+
show the reaction diagram
-
-
-
?
(S)-2-acetolactate + NADPH + H+
2,3-dihydroxy-3-methylbutanoate + NADP+
show the reaction diagram
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.026 - 1.08
NADH
0.013 - 1.4
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 4.3
NADH
0.2 - 7.2
NADPH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.3 - 165
NADH
0.4 - 569
NADPH
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A71S
mutant engineered to use NADH instead of NADPH
A71S/R76D/S78D/Q110A
mutant engineered to use NADH instead of NADPH
A71S/R76D/S78D/Q110V
A71S/R76D/S78D/Q110V/D146G/G185R/K433E
mutant engineered for reversal in cofactor specificity for NADH over NADPH
Q110A
mutant engineered to use NADH instead of NADPH
Q110V
mutant engineered to use NADH instead of NADPH
R76D
mutant engineered to use NADH instead of NADPH
S78D
mutant engineered to use NADH instead of NADPH
S78D/Q110V
mutant engineered to use NADH instead of NADPH
additional information
recipe for altering the cofactor specificity of the ketol-acid reductoisomerases (KARIs). Combining results for an engineered NADH-dependent variant of Escherichia coli KARI with available KARI crystal structures and a comprehensive KARI-sequence alignment, key cofactor specificity determinants are identified and used to construct KARIs with reversed cofactor preference
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biofuel production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wu, W.; Tran-Gyamfi, M.; Jaryenneh, J.; Davis, R.
Cofactor engineering of ketol-acid reductoisomerase (IlvC) and alcohol dehydrogenase (YqhD) improves the fusel alcohol yield in algal protein anaerobic fermentation
Algal Res.
19
162-167
2016
Escherichia coli (P05793)
-
Manually annotated by BRENDA team
Milne, N.; Wahl, S.; van Maris, A.; Pronk, J.; Daran, J.
Excessive by-product formation: A key contributor to low isobutanol yields of engineered
Metab. Eng. Commun.
3
39-51
2016
Escherichia coli (P05793)
Manually annotated by BRENDA team
Bastian, S.; Liu, X.; Meyerowitz, J.; Snow, C.; Chen, M.; Arnold, F.
Engineered ketol-acid reductoisomerase and alcohol dehydrogenase enable anaerobic 2-methylpropan-1-ol production at theoretical yield in Escherichia coli
Metab. Eng.
13
345-352
2011
Escherichia coli (P05793)
Manually annotated by BRENDA team
Brinkmann-Chen, S.; Flock, T.; Cahn, J.; Snow, C.; Brustad, E.; McIntosh, J.; Meinhold, P.; Zhang, L.; Arnold, F.
General approach to reversing ketol-acid reductoisomerase cofactor dependence from NADPH to NADH
Proc. Natl. Acad. Sci. USA
110
10946-10951
2013
Escherichia coli (P05793), Lactococcus lactis subsp. lactis (Q02138), Lactococcus lactis subsp. lactis IL1403 (Q02138), Shewanella sp. (A0KS29), Shewanella sp. ANA-3 (A0KS29), Slackia exigua (D0WGK0), Slackia exigua DSM 15923 (D0WGK0)
Manually annotated by BRENDA team