Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ketol-acid reductoisomerase (NADP( )) (KARI) (EC 1.1.1.86) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Ketol-acid reductoisomerase type 2) (Ketol-acid reductoisomerase type II)

 ILVC_ECOLI              Reviewed;         491 AA.
P05793; Q2M883;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 162.
RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:2653423};
Short=KARI {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:2653423};
EC=1.1.1.86 {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:15654896, ECO:0000269|PubMed:21515217, ECO:0000269|PubMed:2653423, ECO:0000269|PubMed:9015391};
AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:2653423};
Short=AHIR {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:2653423};
AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00435};
AltName: Full=Ketol-acid reductoisomerase type 2 {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:16322583};
AltName: Full=Ketol-acid reductoisomerase type II {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:16322583};
Name=ilvC {ECO:0000255|HAMAP-Rule:MF_00435};
OrderedLocusNames=b3774, JW3747;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=K12;
PubMed=3003115;
Wek R.C., Hatfield G.W.;
"Nucleotide sequence and in vivo expression of the ilvY and ilvC genes
in Escherichia coli K12. Transcription from divergent overlapping
promoters.";
J. Biol. Chem. 261:2441-2450(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=1379743; DOI=10.1126/science.1379743;
Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
"Analysis of the Escherichia coli genome: DNA sequence of the region
from 84.5 to 86.5 minutes.";
Science 257:771-778(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / EMG2;
PubMed=9298646; DOI=10.1002/elps.1150180807;
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded
in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[6]
INDUCTION.
PubMed=3062177; DOI=10.1016/0022-2836(88)90199-4;
Wek R.C., Hatfield G.W.;
"Transcriptional activation at adjacent operators in the divergent-
overlapping ilvY and ilvC promoters of Escherichia coli.";
J. Mol. Biol. 203:643-663(1988).
[7]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
SUBCELLULAR LOCATION, AND PATHWAY.
PubMed=2653423; DOI=10.1021/bi00428a012;
Chunduru S.K., Mrachko G.T., Calvo K.C.;
"Mechanism of ketol acid reductoisomerase--steady-state analysis and
metal ion requirement.";
Biochemistry 28:486-493(1989).
[8]
ENZYME REGULATION.
PubMed=2189496; DOI=10.1021/bi00463a027;
Aulabaugh A., Schloss J.V.;
"Oxalyl hydroxamates as reaction-intermediate analogues for ketol-acid
reductoisomerase.";
Biochemistry 29:2824-2830(1990).
[9]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF ARG-68; LYS-69; LYS-75 AND ARG-76.
PubMed=9015391; DOI=10.1006/abbi.1996.9802;
Rane M.J., Calvo K.C.;
"Reversal of the nucleotide specificity of ketol acid reductoisomerase
by site-directed mutagenesis identifies the NADPH binding site.";
Arch. Biochem. Biophys. 338:83-89(1997).
[10]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
MUTAGENESIS OF HIS-132; LYS-155; GLU-213; ASP-217; GLU-221; GLU-389;
GLU-393 AND SER-414, AND SUBSTRATE SPECIFICITY.
PubMed=15654896; DOI=10.1111/j.1742-4658.2004.04506.x;
Tyagi R., Lee Y.T., Guddat L.W., Duggleby R.G.;
"Probing the mechanism of the bifunctional enzyme ketol-acid
reductoisomerase by site-directed mutagenesis of the active site.";
FEBS J. 272:593-602(2005).
[11]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF ALA-71; ARG-76; SER-78 AND GLN-110.
PubMed=21515217; DOI=10.1016/j.ymben.2011.02.004;
Bastian S., Liu X., Meyerowitz J.T., Snow C.D., Chen M.M.,
Arnold F.H.;
"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).
[12]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), AND SUBUNIT.
PubMed=16322583; DOI=10.1110/ps.051791305;
Tyagi R., Duquerroy S., Navaza J., Guddat L.W., Duggleby R.G.;
"The crystal structure of a bacterial class II ketol-acid
reductoisomerase: domain conservation and evolution.";
Protein Sci. 14:3089-3100(2005).
[13]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND
NADP, COFACTOR, AND SUBUNIT.
PubMed=23036858; DOI=10.1016/j.jmb.2012.09.018;
Wong S.H., Lonhienne T.G., Winzor D.J., Schenk G., Guddat L.W.;
"Bacterial and plant ketol-acid reductoisomerases have different
mechanisms of induced fit during the catalytic cycle.";
J. Mol. Biol. 424:168-179(2012).
-!- FUNCTION: Involved in the biosynthesis of branched-chain amino
acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-
acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-
dihydroxy-isovalerate. In the isomerase reaction, S2AL is
rearranged via a Mg-dependent methyl migration to produce 3-
hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction,
this 2-ketoacid undergoes a metal-dependent reduction by NADPH to
yield (R)-2,3-dihydroxy-isovalerate. Also able to use 2-
ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate,
3-hydroxypyruvate, 3-hydroxy-2-ketobutyrate and pyruvate
(PubMed:15654896). {ECO:0000269|PubMed:15654896,
ECO:0000269|PubMed:21515217, ECO:0000269|PubMed:2653423,
ECO:0000269|PubMed:9015391}.
-!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+)
= (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH.
{ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:15654896,
ECO:0000269|PubMed:21515217, ECO:0000269|PubMed:2653423,
ECO:0000269|PubMed:9015391}.
-!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate +
NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH.
{ECO:0000255|HAMAP-Rule:MF_00435}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:15654896, ECO:0000269|PubMed:23036858,
ECO:0000269|PubMed:2653423};
Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
Rule:MF_00435, ECO:0000269|PubMed:23036858,
ECO:0000269|PubMed:2653423};
-!- ENZYME REGULATION: Inhibited by N-hydroxy-N-isopropyloxamate
(IpOHA). {ECO:0000269|PubMed:2189496}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.04 mM for NADPH {ECO:0000269|PubMed:21515217};
KM=0.042 mM for NADP {ECO:0000269|PubMed:9015391};
KM=0.073 mM for NADPH {ECO:0000269|PubMed:9015391};
KM=0.17 mM for 2-ketopantoate (at pH 8 and 37 degrees Celsius)
{ECO:0000269|PubMed:15654896};
KM=0.206 mM for NADH {ECO:0000269|PubMed:9015391};
KM=0.21 mM for 3-hydroxy-2-ketobutyrate (at pH 8 and 37 degrees
Celsius) {ECO:0000269|PubMed:15654896};
KM=0.25 mM for 2-acetolactate (at pH 8 and 37 degrees Celsius)
{ECO:0000269|PubMed:15654896};
KM=0.27 mM for 3-hydroxy-3-methyl-2-ketobutyrate (at pH 8 and 37
degrees Celsius) {ECO:0000269|PubMed:15654896};
KM=0.42 mM for magnesium (with S2AL and NADPH as substrates)
{ECO:0000269|PubMed:2653423};
KM=1.08 mM for NADH {ECO:0000269|PubMed:21515217};
KM=1.54 mM for pyruvate (at pH 8 and 37 degrees Celsius)
{ECO:0000269|PubMed:2653423};
KM=2.96 mM for 3-hydroxypyruvate (at pH 8 and 37 degrees
Celsius) {ECO:0000269|PubMed:2653423};
KM=3.15 mM for 2-ketovalerate (at pH 8 and 37 degrees Celsius)
{ECO:0000269|PubMed:2653423};
KM=4.56 mM for 2-ketobutyrate (at pH 8 and 37 degrees Celsius)
{ECO:0000269|PubMed:2653423};
KM=6.91 mM for 2-ketoisovalerate (at pH 8 and 37 degrees
Celsius) {ECO:0000269|PubMed:2653423};
Vmax=5.421 umol/min/mg enzyme with 3-hydroxypyruvate as
substrate (at pH 8 and 37 degrees Celsius)
{ECO:0000269|PubMed:15654896};
Vmax=3.541 umol/min/mg enzyme with 3-hydroxy-3-methyl-2-
ketobutyrate as substrate (at pH 8 and 37 degrees Celsius)
{ECO:0000269|PubMed:15654896};
Vmax=2.25 umol/min/mg enzyme with 2-acetolactate as substrate
(at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896};
Vmax=0.599 umol/min/mg enzyme with 3-hydroxy-2-ketobutyrate as
substrate (at pH 8 and 37 degrees Celsius)
{ECO:0000269|PubMed:15654896};
Vmax=0.196 umol/min/mg enzyme with 2-ketopantoate as substrate
(at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896};
Vmax=0.184 umol/min/mg enzyme with 2-ketoisovalerate as
substrate (at pH 8 and 37 degrees Celsius)
{ECO:0000269|PubMed:15654896};
Vmax=0.168 umol/min/mg enzyme with 2-ketobutyrate as substrate
(at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896};
Vmax=0.05 umol/min/mg enzyme with 2-ketovalerate as substrate
(at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896};
Vmax=0.021 umol/min/mg enzyme with pyruvate as substrate (at pH
8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896};
Note=Kcat is 7.2 min(-1) for reductoisomerase activity with
NADPH as substrate (PubMed:9015391). Kcat is 3.1 min(-1) for
reductoisomerase activity with NADPH as substrate
(PubMed:9015391). Kcat is 0.11 min(-1) for reductoisomerase
activity with NADH as substrate (PubMed:9015391). Kcat is 5.376
sec(-1) for reductoisomerase activity with 3-hydroxypyruvate as
substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896).
Kcat is 3.6 sec(-1) for reductoisomerase activity with NADPH as
substrate (PubMed:21515217). Kcat is 3.511 sec(-1) for
reductoisomerase activity with 3-hydroxy-3-methyl-2-ketobutyrate
as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896).
Kcat is 2.231 sec(-1) for reductoisomerase activity with 2-
acetolactate as substrate (at pH 8 and 37 degrees Celsius)
(PubMed:15654896). Kcat is 0.594 sec(-1) for reductoisomerase
activity with 3-hydroxy-2-ketobutyrate as substrate (at pH 8 and
37 degrees Celsius) (PubMed:15654896). Kcat is 0.3 sec(-1) for
reductoisomerase activity with NADH as substrate
(PubMed:21515217). Kcat is 0.194 sec(-1) for reductoisomerase
activity with 2-ketopantoate as substrate (at pH 8 and 37
degrees Celsius) (PubMed:15654896). Kcat is 0.182 sec(-1) for
reductoisomerase activity with 2-ketoisovalerate as substrate
(at pH 8 and 37 degrees Celsius) (PubMed:15654896). Kcat is
0.167 sec(-1) for reductoisomerase activity with 2-ketobutyrate
as substrate (at pH 8 and 37 degrees Celsius) (PubMed:15654896).
Kcat is 0.05 sec(-1) for reductoisomerase activity with 2-
ketovalerate as substrate (at pH 8 and 37 degrees Celsius)
(PubMed:15654896). Kcat is 0.021 sec(-1) for reductoisomerase
activity with pyruvate as substrate (at pH 8 and 37 degrees
Celsius) (PubMed:15654896). {ECO:0000269|PubMed:15654896,
ECO:0000269|PubMed:21515217, ECO:0000269|PubMed:9015391};
-!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
Rule:MF_00435, ECO:0000305|PubMed:2653423}.
-!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000305|PubMed:2653423}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16322583,
ECO:0000269|PubMed:23036858}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:2653423}.
-!- INDUCTION: In the presence of acetohydroxybutyrate and
acetolactate and by the activator IlvY.
{ECO:0000269|PubMed:3003115, ECO:0000269|PubMed:3062177}.
-!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
{ECO:0000255|HAMAP-Rule:MF_00435}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M11689; AAA24029.1; -; Genomic_DNA.
EMBL; M87049; AAA67577.1; -; Genomic_DNA.
EMBL; U00096; AAC76779.1; -; Genomic_DNA.
EMBL; AP009048; BAE77523.1; -; Genomic_DNA.
PIR; A65181; ISECKR.
RefSeq; NP_418222.1; NC_000913.3.
RefSeq; WP_000024939.1; NZ_LN832404.1.
PDB; 1YRL; X-ray; 2.60 A; A/B/C/D=1-491.
PDB; 3ULK; X-ray; 2.30 A; A/B=1-491.
PDBsum; 1YRL; -.
PDBsum; 3ULK; -.
ProteinModelPortal; P05793; -.
SMR; P05793; -.
BioGrid; 4263331; 5.
IntAct; P05793; 4.
STRING; 316385.ECDH10B_3963; -.
BindingDB; P05793; -.
ChEMBL; CHEMBL2366462; -.
SWISS-2DPAGE; P05793; -.
PaxDb; P05793; -.
PRIDE; P05793; -.
EnsemblBacteria; AAC76779; AAC76779; b3774.
EnsemblBacteria; BAE77523; BAE77523; BAE77523.
GeneID; 948286; -.
KEGG; ecj:JW3747; -.
KEGG; eco:b3774; -.
PATRIC; fig|511145.12.peg.3891; -.
EchoBASE; EB0490; -.
EcoGene; EG10495; ilvC.
eggNOG; ENOG4105C6M; Bacteria.
eggNOG; COG0059; LUCA.
HOGENOM; HOG000286135; -.
InParanoid; P05793; -.
KO; K00053; -.
PhylomeDB; P05793; -.
BioCyc; EcoCyc:KETOLREDUCTOISOM-MONOMER; -.
BioCyc; MetaCyc:KETOLREDUCTOISOM-MONOMER; -.
BRENDA; 1.1.1.86; 2026.
UniPathway; UPA00047; UER00056.
UniPathway; UPA00049; UER00060.
EvolutionaryTrace; P05793; -.
PRO; PR:P05793; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0004455; F:ketol-acid reductoisomerase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
GO; GO:0009097; P:isoleucine biosynthetic process; IDA:EcoCyc.
GO; GO:0009099; P:valine biosynthetic process; IDA:EcoCyc.
Gene3D; 1.10.1040.10; -; 1.
HAMAP; MF_00435; IlvC; 1.
InterPro; IPR008927; 6-PGluconate_DH_C-like.
InterPro; IPR013328; 6PGD_dom_2.
InterPro; IPR000506; AcH_isomrdctse_C.
InterPro; IPR013116; IlvN.
InterPro; IPR013023; KARI.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR21371; PTHR21371; 2.
Pfam; PF01450; IlvC; 2.
Pfam; PF07991; IlvN; 1.
SUPFAM; SSF48179; SSF48179; 2.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00465; ilvC; 1.
1: Evidence at protein level;
3D-structure; Amino-acid biosynthesis;
Branched-chain amino acid biosynthesis; Complete proteome; Cytoplasm;
Direct protein sequencing; Magnesium; Metal-binding; NADP;
Nucleotide-binding; Oxidoreductase; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9298646}.
CHAIN 2 491 Ketol-acid reductoisomerase (NADP(+)).
/FTId=PRO_0000151309.
DOMAIN 35 204 IlvN. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000305|PubMed:16322583}.
DOMAIN 210 342 IlvC 1. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000305|PubMed:16322583}.
DOMAIN 357 482 IlvC 2. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000305|PubMed:16322583}.
NP_BIND 45 48 NADP. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:23036858}.
NP_BIND 108 110 NADP. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:23036858}.
ACT_SITE 132 132 {ECO:0000255|HAMAP-Rule:MF_00435}.
METAL 217 217 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_00435,
ECO:0000269|PubMed:23036858}.
METAL 217 217 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_00435,
ECO:0000269|PubMed:23036858}.
METAL 221 221 Magnesium 1. {ECO:0000255|HAMAP-
Rule:MF_00435}.
METAL 389 389 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_00435,
ECO:0000269|PubMed:23036858}.
METAL 393 393 Magnesium 2. {ECO:0000255|HAMAP-
Rule:MF_00435,
ECO:0000269|PubMed:23036858}.
BINDING 68 68 NADP. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000305|PubMed:9015391}.
BINDING 76 76 NADP. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:23036858,
ECO:0000305|PubMed:9015391}.
BINDING 78 78 NADP. {ECO:0000255|HAMAP-Rule:MF_00435,
ECO:0000269|PubMed:23036858}.
BINDING 158 158 NADP; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00435}.
BINDING 414 414 Substrate. {ECO:0000255|HAMAP-
Rule:MF_00435}.
MUTAGEN 68 68 R->D: Inversion of cofactor specificity
from NADPH to NADH; when associated with
L-69, V-75 and D-76.
{ECO:0000269|PubMed:9015391}.
MUTAGEN 68 68 R->Q: 18-fold decrease of the catalytic
efficiency and 3-fold decrease of the
affinity for NADPH.
{ECO:0000269|PubMed:9015391}.
MUTAGEN 69 69 K->L: Does not significantly alter the
affinity for NADPH. Slight increase of
the catalytic efficiency. Inversion of
cofactor specificity from NADPH to NADH;
when associated with D-68, V-75 and D-76.
{ECO:0000269|PubMed:9015391}.
MUTAGEN 71 71 A->S: 7- and 2.5-fold increase of the
reductoisomerase activity with NADH and
NADPH, respectively.
{ECO:0000269|PubMed:21515217}.
MUTAGEN 75 75 K->Q: 13-fold decrease of the catalytic
efficiency and 3-fold increase of the
affinity for NADPH.
{ECO:0000269|PubMed:9015391}.
MUTAGEN 75 75 K->V: Inversion of cofactor specificity
from NADPH to NADH; when associated with
D-68, L-69 and D-76.
{ECO:0000269|PubMed:9015391}.
MUTAGEN 76 76 R->D: 3-fold increase of the
reductoisomerase activity with NADH and
slight decrease of the reductoisomerase
activity with NADPH.
{ECO:0000269|PubMed:21515217}.
MUTAGEN 76 76 R->D: Strong increase of catalytic
efficiency and 2.5-fold increase of the
affinity for NADH. 4-fold decrease of the
catalytic efficiency and strong decrease
of the affinity for NADPH. Inversion of
cofactor specificity from NADPH to NADH;
when associated with D-68, L-69 and V-75.
{ECO:0000269|PubMed:9015391}.
MUTAGEN 76 76 R->Q: 20-fold decrease of the catalytic
efficiency and 5-fold decrease of the
affinity for NADPH.
{ECO:0000269|PubMed:9015391}.
MUTAGEN 78 78 S->D: 12-fold increase of the
reductoisomerase activity with NADH and
slight decrease of the reductoisomerase
activity with NADPH.
{ECO:0000269|PubMed:21515217}.
MUTAGEN 110 110 Q->V,A: 12- and 2-fold increase of the
reductoisomerase activity with NADH and
NADPH, respectively.
{ECO:0000269|PubMed:21515217}.
MUTAGEN 132 132 H->K: Loss of reductoisomerase activity.
{ECO:0000269|PubMed:15654896}.
MUTAGEN 132 132 H->Q: Loss of reductoisomerase activity.
The reductase activity with 3-
hydroxypyruvate and HMKB is nearly
normal, and the isomerase activity
decreases 24-fold.
{ECO:0000269|PubMed:15654896}.
MUTAGEN 155 155 K->E,Q: Loss of reductoisomerase
activity. {ECO:0000269|PubMed:15654896}.
MUTAGEN 155 155 K->R: Loss of reductoisomerase activity.
The reductase activity with 3-
hydroxypyruvate and HMKB is nearly
normal, and the isomerase activity
decreases 40-fold.
{ECO:0000269|PubMed:15654896}.
MUTAGEN 213 213 E->D: Loss of reductoisomerase activity.
1.5-fold decrease of the reductase
activity with 3-hydroxypyruvate and the
isomerase activity decreases 48-fold.
{ECO:0000269|PubMed:15654896}.
MUTAGEN 217 217 D->E,N: Loss of reductoisomerase
activity. {ECO:0000269|PubMed:15654896}.
MUTAGEN 221 221 E->D,Q: Loss of reductoisomerase
activity. {ECO:0000269|PubMed:15654896}.
MUTAGEN 389 389 E->D: Loss of reductoisomerase activity.
1.5-fold decrease of the reductase
activity with 3-hydroxypyruvate and the
isomerase activity decreases 4-fold.
{ECO:0000269|PubMed:15654896}.
MUTAGEN 389 389 E->Q: Loss of reductoisomerase activity.
{ECO:0000269|PubMed:15654896}.
MUTAGEN 393 393 E->D: Loss of reductoisomerase activity.
The reductase activity with HMKB is
nearly normal.
{ECO:0000269|PubMed:15654896}.
MUTAGEN 414 414 S->A: Loss of reductoisomerase activity.
The isomerase activity decreases 15-fold.
{ECO:0000269|PubMed:15654896}.
MUTAGEN 414 414 S->T: Loss of reductoisomerase activity.
The isomerase activity decreases 24-fold.
{ECO:0000269|PubMed:15654896}.
CONFLICT 251 251 E -> K (in Ref. 1; AAA24029).
{ECO:0000305}.
HELIX 5 7 {ECO:0000244|PDB:3ULK}.
HELIX 10 17 {ECO:0000244|PDB:3ULK}.
STRAND 20 22 {ECO:0000244|PDB:1YRL}.
HELIX 25 28 {ECO:0000244|PDB:3ULK}.
TURN 29 32 {ECO:0000244|PDB:3ULK}.
HELIX 33 35 {ECO:0000244|PDB:3ULK}.
STRAND 38 44 {ECO:0000244|PDB:3ULK}.
HELIX 47 58 {ECO:0000244|PDB:3ULK}.
STRAND 62 67 {ECO:0000244|PDB:3ULK}.
HELIX 69 73 {ECO:0000244|PDB:3ULK}.
HELIX 77 84 {ECO:0000244|PDB:3ULK}.
STRAND 88 91 {ECO:0000244|PDB:3ULK}.
HELIX 92 95 {ECO:0000244|PDB:3ULK}.
HELIX 96 98 {ECO:0000244|PDB:3ULK}.
STRAND 100 104 {ECO:0000244|PDB:3ULK}.
HELIX 108 110 {ECO:0000244|PDB:3ULK}.
HELIX 111 118 {ECO:0000244|PDB:3ULK}.
HELIX 119 121 {ECO:0000244|PDB:3ULK}.
STRAND 127 132 {ECO:0000244|PDB:3ULK}.
HELIX 134 137 {ECO:0000244|PDB:3ULK}.
STRAND 147 156 {ECO:0000244|PDB:3ULK}.
HELIX 158 166 {ECO:0000244|PDB:3ULK}.
STRAND 173 177 {ECO:0000244|PDB:3ULK}.
HELIX 179 181 {ECO:0000244|PDB:3ULK}.
HELIX 187 197 {ECO:0000244|PDB:3ULK}.
HELIX 200 202 {ECO:0000244|PDB:3ULK}.
STRAND 205 207 {ECO:0000244|PDB:3ULK}.
HELIX 210 222 {ECO:0000244|PDB:3ULK}.
TURN 223 226 {ECO:0000244|PDB:3ULK}.
HELIX 227 242 {ECO:0000244|PDB:3ULK}.
HELIX 247 275 {ECO:0000244|PDB:3ULK}.
HELIX 279 309 {ECO:0000244|PDB:3ULK}.
HELIX 311 321 {ECO:0000244|PDB:3ULK}.
TURN 322 324 {ECO:0000244|PDB:3ULK}.
HELIX 325 336 {ECO:0000244|PDB:3ULK}.
HELIX 338 341 {ECO:0000244|PDB:3ULK}.
HELIX 351 356 {ECO:0000244|PDB:3ULK}.
HELIX 359 377 {ECO:0000244|PDB:3ULK}.
TURN 378 380 {ECO:0000244|PDB:3ULK}.
HELIX 383 388 {ECO:0000244|PDB:3ULK}.
HELIX 391 393 {ECO:0000244|PDB:3ULK}.
HELIX 394 412 {ECO:0000244|PDB:3ULK}.
HELIX 415 431 {ECO:0000244|PDB:3ULK}.
HELIX 433 437 {ECO:0000244|PDB:3ULK}.
STRAND 443 446 {ECO:0000244|PDB:3ULK}.
HELIX 455 466 {ECO:0000244|PDB:3ULK}.
HELIX 469 487 {ECO:0000244|PDB:3ULK}.
SEQUENCE 491 AA; 54069 MW; 9CA34BA61C9AEBBA CRC64;
MANYFNTLNL RQQLAQLGKC RFMGRDEFAD GASYLQGKKV VIVGCGAQGL NQGLNMRDSG
LDISYALRKE AIAEKRASWR KATENGFKVG TYEELIPQAD LVINLTPDKQ HSDVVRTVQP
LMKDGAALGY SHGFNIVEVG EQIRKDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE
NDPKGEGMAI AKAWAAATGG HRAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSLLCFDKL
VEEGTDPAYA EKLIQFGWET ITEALKQGGI TLMMDRLSNP AKLRAYALSE QLKEIMAPLF
QKHMDDIISG EFSSGMMADW ANDDKKLLTW REETGKTAFE TAPQYEGKIG EQEYFDKGVL
MIAMVKAGVE LAFETMVDSG IIEESAYYES LHELPLIANT IARKRLYEMN VVISDTAEYG
NYLFSYACVP LLKPFMAELQ PGDLGKAIPE GAVDNGQLRD VNEAIRSHAI EQVGKKLRGY
MTDMKRIAVA G


Related products :

Catalog number Product name Quantity
orb60878 Fumalic acid Fumalic acid(Ferulic acid) is a hydroxycinnamic acid and a type of organic compound found in the Ferula assafoetida L. or Ligusticum chuanxiong. For research use only. 10 mg
EIAAB28640 BCKADE2,BCKAD-E2,Bos taurus,Bovine,Branched-chain alpha-keto acid dehydrogenase complex component E2,DBT,Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase co
U0902m CLIA Acp5,Mouse,Mus musculus,T5ap,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,Trap,TR-AP,TrATPase,Type 5 acid phosphatase 96T
E0902m ELISA kit Acp5,Mouse,Mus musculus,T5ap,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,Trap,TR-AP,TrATPase,Type 5 acid phosphatase 96T
E0902m ELISA Acp5,Mouse,Mus musculus,T5ap,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,Trap,TR-AP,TrATPase,Type 5 acid phosphatase 96T
U0902Rb CLIA ACP5,Oryctolagus cuniculus,Rabbit,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase 96T
U0902h CLIA ACP5,Homo sapiens,Human,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase 96T
E0902Rb ELISA ACP5,Oryctolagus cuniculus,Rabbit,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase 96T
E0902h ELISA ACP5,Homo sapiens,Human,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase 96T
E0902h ELISA kit ACP5,Homo sapiens,Human,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase 96T
E0902Rb ELISA kit ACP5,Oryctolagus cuniculus,Rabbit,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase 96T
H-1775.0025 (Arg8)_Vasopressin (free acid) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym Leiormone (free acid), Pitressin (free acid), AVP (free acid), Arginine Antidiuretic Hormone (free acid), Argip 25.0 mg
H-1775.0005 (Arg8)_Vasopressin (free acid) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym Leiormone (free acid), Pitressin (free acid), AVP (free acid), Arginine Antidiuretic Hormone (free acid), Argip 5.0 mg
H-1775.0025 (Arg8)_Vasopressin (free acid) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym Leiormone (free acid), Pitressin (free acid), AVP (free acid), Arginine Antidiuretic Hormone (free acid), Argip 25.0 mg
H-1775.0005 (Arg8)_Vasopressin (free acid) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym Leiormone (free acid), Pitressin (free acid), AVP (free acid), Arginine Antidiuretic Hormone (free acid), Argip 5.0 mg
U0902p CLIA ACP5,Pig,Sus scrofa,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase,UF,Uteroferrin 96T
E0902p ELISA kit ACP5,Pig,Sus scrofa,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase,UF,Uteroferrin 96T
E0902r ELISA Acp5,Rat,Rattus norvegicus,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase 96T
E0902r ELISA kit Acp5,Rat,Rattus norvegicus,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase 96T
E0902p ELISA ACP5,Pig,Sus scrofa,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase,UF,Uteroferrin 96T
U0902r CLIA Acp5,Rat,Rattus norvegicus,Tartrate-resistant acid ATPase,Tartrate-resistant acid phosphatase type 5,TR-AP,TrATPase,Type 5 acid phosphatase 96T
EIAAB28639 BCATE2,BCKADE2,BCKAD-E2,Branched-chain alpha-keto acid dehydrogenase complex component E2,DBT,Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex,Dihyd
2112-20 Acetic Acid (50 mM) Ethanoic acid, methanecarboxylic acid, ethylic acid 20 ml
2112-2 Acetic Acid (50 mM) Ethanoic acid, methanecarboxylic acid, ethylic acid 2 ml
CSB-EL002606RA Rat branched chain keto acid dehydrogenase E1, beta polypeptide (BCKDHB) ELISA kit, Species Rat, Sample Type serum, plasma 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur