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Glyceraldehyde-3-phosphate dehydrogenase A (GAPDH-A) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase)

 G3P1_ECOLI              Reviewed;         331 AA.
P0A9B2; P06977;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 121.
RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase A {ECO:0000303|PubMed:2659073};
Short=GAPDH-A {ECO:0000303|PubMed:2659073};
EC=1.2.1.12 {ECO:0000269|PubMed:2659073};
AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000303|PubMed:2659073};
Name=gapA {ECO:0000303|PubMed:2659073};
OrderedLocusNames=b1779, JW1768;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2990926; DOI=10.1111/j.1432-1033.1985.tb08988.x;
Branlant G., Branlant C.;
"Nucleotide sequence of the Escherichia coli gap gene. Different
evolutionary behavior of the NAD+-binding domain and of the catalytic
domain of D-glyceraldehyde-3-phosphate dehydrogenase.";
Eur. J. Biochem. 150:61-66(1985).
[2]
SEQUENCE REVISION TO 295-300.
Nelson K.;
Submitted (SEP-1990) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M.,
Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K.,
Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N.,
Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J.,
Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.;
"A 570-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 28.0-40.1 min region on the linkage map.";
DNA Res. 3:363-377(1996).
[4]
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).
[5]
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).
[6]
PROTEIN SEQUENCE OF 2-13.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J.,
Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A.,
Hochstrasser D.F.;
Submitted (SEP-1994) to UniProtKB.
[7]
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).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 7-314.
STRAIN=A8190, E2666-74, E3406, E830587, E851819, ECOR 14, ECOR 32,
ECOR 40, ECOR 52, ECOR 58, ECOR 64, and ECOR 70;
PubMed=1862091; DOI=10.1073/pnas.88.15.6667;
Nelson K., Whittam T.S., Selander R.K.;
"Nucleotide polymorphism and evolution in the glyceraldehyde-3-
phosphate dehydrogenase gene (gapA) in natural populations of
Salmonella and Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 88:6667-6671(1991).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-321.
STRAIN=ECOR 10, ECOR 16, ECOR 38, ECOR 39, ECOR 4, ECOR 40, ECOR 49,
ECOR 65, ECOR 68, ECOR 8, and O2:HN / ECOR 50 / P97 / UPEC;
PubMed=7896119;
Guttman D.S., Dykhuizen D.E.;
"Detecting selective sweeps in naturally occurring Escherichia coli.";
Genetics 138:993-1003(1994).
[10]
GENE TRANSFER DISCUSSION.
PubMed=2124629; DOI=10.1007/BF02106053;
Doolittle R.F., Feng D.F., Anderson K.L., Alberro M.R.;
"A naturally occurring horizontal gene transfer from a eukaryote to a
prokaryote.";
J. Mol. Evol. 31:383-388(1990).
[11]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
MUTAGENESIS OF HIS-177.
PubMed=2659073; DOI=10.1021/bi00432a036;
Soukri A., Mougin A., Corbier C., Wonacott A., Branlant C.,
Branlant G.;
"Role of the histidine 176 residue in glyceraldehyde-3-phosphate
dehydrogenase as probed by site-directed mutagenesis.";
Biochemistry 28:2586-2592(1989).
[12]
IDENTIFICATION BY 2D-GEL.
PubMed=9298644; DOI=10.1002/elps.1150180805;
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
Neidhardt F.C.;
"Escherichia coli proteome analysis using the gene-protein database.";
Electrophoresis 18:1243-1251(1997).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132; LYS-138; LYS-192 AND
LYS-249, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved
modification in Escherichia coli.";
Mol. Cell. Proteomics 8:215-225(2009).
[14]
MALONYLATION AT LYS-331.
STRAIN=K12;
PubMed=21908771; DOI=10.1074/mcp.M111.012658;
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
Dai J., Verdin E., Ye Y., Zhao Y.;
"The first identification of lysine malonylation substrates and its
regulatory enzyme.";
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
[15]
SUCCINYLATION AT LYS-115; LYS-124; LYS-132; LYS-192; LYS-213; LYS-217;
LYS-225; LYS-249; LYS-257; LYS-261 AND LYS-331.
STRAIN=K12;
PubMed=21151122; DOI=10.1038/nchembio.495;
Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.;
"Identification of lysine succinylation as a new post-translational
modification.";
Nat. Chem. Biol. 7:58-63(2011).
[16]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF WILD-TYPE AND THR-313 MUTANT
IN COMPLEX WITH NAD, AND SUBUNIT.
PubMed=8636984; DOI=10.1006/jmbi.1996.0204;
Duee E., Olivier-Deyris L., Fanchon E., Corbier C., Branlant G.,
Dideberg O.;
"Comparison of the structures of wild-type and a N313T mutant of
Escherichia coli glyceraldehyde 3-phosphate dehydrogenases:
implication for NAD binding and cooperativity.";
J. Mol. Biol. 257:814-838(1996).
[17]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH NAD AND
GLYCERALDEHYDE 3-PHOSPHATE, AND SUBUNIT.
PubMed=10978154; DOI=10.1021/bi9927080;
Yun M., Park C.-G., Kim J.-Y., Park H.-W.;
"Structural analysis of glyceraldehyde 3-phosphate dehydrogenase from
Escherichia coli: direct evidence of substrate binding and cofactor-
induced conformational changes.";
Biochemistry 39:10702-10710(2000).
[18]
X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) IN COMPLEX WITH SUBSTRATE
ANALOG.
Shin D.H., Thor J., Yokota H., Kim R., Kim S.H.;
"Crystal structure of MES buffer bound form of glyceraldehyde 3-
phosphate dehydrogenase from Escherichia coli.";
Submitted (JAN-2004) to the PDB data bank.
[19]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NAD AND
SUBSTRATE ANALOG, AND SUBUNIT.
PubMed=19542219; DOI=10.1074/jbc.M109.004648;
Frayne J., Taylor A., Cameron G., Hadfield A.T.;
"Structure of insoluble rat sperm glyceraldehyde-3-phosphate
dehydrogenase (GAPDH) via heterotetramer formation with Escherichia
coli GAPDH reveals target for contraceptive design.";
J. Biol. Chem. 284:22703-22712(2009).
-!- FUNCTION: Catalyzes the oxidative phosphorylation of
glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG)
using the cofactor NAD. The first reaction step involves the
formation of a hemiacetal intermediate between G3P and a cysteine
residue, and this hemiacetal intermediate is then oxidized to a
thioester, with concomitant reduction of NAD to NADH. The reduced
NADH is then exchanged with the second NAD, and the thioester is
attacked by a nucleophilic inorganic phosphate to produce BPG.
{ECO:0000269|PubMed:2659073}.
-!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
{ECO:0000269|PubMed:2659073}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=15 uM for BPG {ECO:0000269|PubMed:2659073};
KM=42 uM for NAD {ECO:0000269|PubMed:2659073};
KM=1500 uM for G3P {ECO:0000269|PubMed:2659073};
Note=Kcat is 1056 sec(-1) for dehydrogenase activity.;
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10978154,
ECO:0000269|PubMed:19542219, ECO:0000269|PubMed:8636984}.
-!- INTERACTION:
P0A9H9:cheZ; NbExp=2; IntAct=EBI-368904, EBI-546726;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
dehydrogenase family. {ECO:0000305}.
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EMBL; X02662; CAA26498.1; -; Genomic_DNA.
EMBL; U00096; AAC74849.1; -; Genomic_DNA.
EMBL; AP009048; BAA15576.1; -; Genomic_DNA.
EMBL; M66870; AAA23838.1; -; Genomic_DNA.
EMBL; M66871; AAA23839.1; -; Genomic_DNA.
EMBL; M66872; AAA02930.1; -; Genomic_DNA.
EMBL; M66873; AAA23840.1; -; Genomic_DNA.
EMBL; M66874; AAA23841.1; -; Genomic_DNA.
EMBL; M66875; AAA23842.1; -; Genomic_DNA.
EMBL; M66876; AAA23843.1; -; Genomic_DNA.
EMBL; M66877; AAA23844.1; -; Genomic_DNA.
EMBL; M66878; AAA23845.1; -; Genomic_DNA.
EMBL; M66879; AAA23846.1; -; Genomic_DNA.
EMBL; M66880; AAA23847.1; -; Genomic_DNA.
EMBL; M66881; AAA23848.1; -; Genomic_DNA.
EMBL; M66882; AAA23849.1; -; Genomic_DNA.
EMBL; U07750; AAC43271.1; -; Genomic_DNA.
EMBL; U07751; AAC43272.1; -; Genomic_DNA.
EMBL; U07752; AAC43273.1; -; Genomic_DNA.
EMBL; U07754; AAC43274.1; -; Genomic_DNA.
EMBL; U07765; AAC43284.1; -; Genomic_DNA.
EMBL; U07768; AAC43285.1; -; Genomic_DNA.
EMBL; U07769; AAC43286.1; -; Genomic_DNA.
EMBL; U07770; AAC43287.1; -; Genomic_DNA.
EMBL; U07771; AAC43288.1; -; Genomic_DNA.
EMBL; U07772; AAC43289.1; -; Genomic_DNA.
EMBL; U07773; AAC43290.1; -; Genomic_DNA.
PIR; A25209; DEECG3.
RefSeq; NP_416293.1; NC_000913.3.
RefSeq; WP_000153502.1; NZ_LN832404.1.
PDB; 1DC3; X-ray; 2.50 A; A/B=2-331.
PDB; 1DC4; X-ray; 2.50 A; A/B=2-331.
PDB; 1DC5; X-ray; 2.00 A; A/B=2-331.
PDB; 1DC6; X-ray; 2.00 A; A/B=2-331.
PDB; 1GAD; X-ray; 1.80 A; O/P=2-331.
PDB; 1GAE; X-ray; 2.17 A; O/P=2-331.
PDB; 1S7C; X-ray; 2.04 A; A=1-331.
PDB; 2VYN; X-ray; 2.20 A; A/B/C=1-331.
PDB; 2VYV; X-ray; 2.38 A; A/B/C=1-331.
PDBsum; 1DC3; -.
PDBsum; 1DC4; -.
PDBsum; 1DC5; -.
PDBsum; 1DC6; -.
PDBsum; 1GAD; -.
PDBsum; 1GAE; -.
PDBsum; 1S7C; -.
PDBsum; 2VYN; -.
PDBsum; 2VYV; -.
ProteinModelPortal; P0A9B2; -.
SMR; P0A9B2; -.
BioGrid; 4260308; 24.
BioGrid; 851992; 1.
DIP; DIP-31848N; -.
IntAct; P0A9B2; 27.
MINT; MINT-1255410; -.
STRING; 316385.ECDH10B_1917; -.
DrugBank; DB03814; 2-(N-Morpholino)-Ethanesulfonic Acid.
DrugBank; DB02263; Glyceraldehyde-3-Phosphate.
iPTMnet; P0A9B2; -.
SWISS-2DPAGE; P0A9B2; -.
PaxDb; P0A9B2; -.
PRIDE; P0A9B2; -.
EnsemblBacteria; AAC74849; AAC74849; b1779.
EnsemblBacteria; BAA15576; BAA15576; BAA15576.
GeneID; 947679; -.
KEGG; ecj:JW1768; -.
KEGG; eco:b1779; -.
PATRIC; fig|1411691.4.peg.475; -.
EchoBASE; EB0362; -.
EcoGene; EG10367; gapA.
eggNOG; ENOG4105C17; Bacteria.
eggNOG; COG0057; LUCA.
HOGENOM; HOG000071678; -.
InParanoid; P0A9B2; -.
KO; K00134; -.
PhylomeDB; P0A9B2; -.
BioCyc; EcoCyc:GAPDH-A-MONOMER; -.
BioCyc; MetaCyc:GAPDH-A-MONOMER; -.
BRENDA; 1.2.1.12; 2026.
SABIO-RK; P0A9B2; -.
UniPathway; UPA00109; UER00184.
EvolutionaryTrace; P0A9B2; -.
PRO; PR:P0A9B2; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:UniProtKB.
GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; IMP:EcoCyc.
InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
InterPro; IPR020830; GlycerAld_3-P_DH_AS.
InterPro; IPR020829; GlycerAld_3-P_DH_cat.
InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR10836; PTHR10836; 1.
Pfam; PF02800; Gp_dh_C; 1.
Pfam; PF00044; Gp_dh_N; 1.
PIRSF; PIRSF000149; GAP_DH; 1.
PRINTS; PR00078; G3PDHDRGNASE.
SMART; SM00846; Gp_dh_N; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01534; GAPDH-I; 1.
PROSITE; PS00071; GAPDH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycolysis; NAD; Nucleotide-binding;
Oxidoreductase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:9298646,
ECO:0000269|Ref.6}.
CHAIN 2 331 Glyceraldehyde-3-phosphate dehydrogenase
A.
/FTId=PRO_0000145648.
NP_BIND 12 13 NAD. {ECO:0000269|PubMed:10978154,
ECO:0000269|PubMed:19542219,
ECO:0000269|PubMed:8636984,
ECO:0000269|Ref.18}.
REGION 149 151 Glyceraldehyde 3-phosphate binding.
{ECO:0000269|PubMed:10978154}.
REGION 209 210 Glyceraldehyde 3-phosphate binding.
{ECO:0000269|PubMed:10978154}.
ACT_SITE 150 150 Nucleophile.
{ECO:0000305|PubMed:10978154}.
BINDING 34 34 NAD. {ECO:0000269|PubMed:10978154,
ECO:0000269|PubMed:19542219,
ECO:0000269|PubMed:8636984}.
BINDING 78 78 NAD; via carbonyl oxygen.
{ECO:0000269|PubMed:10978154,
ECO:0000269|PubMed:19542219}.
BINDING 120 120 NAD. {ECO:0000269|PubMed:19542219}.
BINDING 180 180 Glyceraldehyde 3-phosphate.
{ECO:0000250|UniProtKB:P00362}.
BINDING 232 232 Glyceraldehyde 3-phosphate.
{ECO:0000269|PubMed:19542219,
ECO:0000269|Ref.18,
ECO:0000305|PubMed:10978154}.
BINDING 314 314 NAD. {ECO:0000269|PubMed:10978154,
ECO:0000269|PubMed:19542219,
ECO:0000269|PubMed:8636984}.
SITE 177 177 Activates thiol group during catalysis.
{ECO:0000269|PubMed:2659073}.
MOD_RES 115 115 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 124 124 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 132 132 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:18723842}.
MOD_RES 132 132 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:21151122}.
MOD_RES 138 138 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 192 192 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:18723842}.
MOD_RES 192 192 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:21151122}.
MOD_RES 213 213 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 217 217 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 225 225 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 249 249 N6-acetyllysine.
{ECO:0000269|PubMed:18723842}.
MOD_RES 249 249 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 257 257 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 261 261 N6-succinyllysine.
{ECO:0000269|PubMed:21151122}.
MOD_RES 331 331 N6-malonyllysine; alternate.
{ECO:0000269|PubMed:21908771}.
MOD_RES 331 331 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:21151122}.
VARIANT 43 43 Y -> I (in strain: ECOR 70).
VARIANT 266 266 G -> D (in strain: E830587).
VARIANT 267 267 E -> A (in strain: E2666-74).
MUTAGEN 177 177 H->N: Reduces activity about 50-fold.
{ECO:0000269|PubMed:2659073}.
STRAND 3 8 {ECO:0000244|PDB:1GAD}.
HELIX 12 22 {ECO:0000244|PDB:1GAD}.
STRAND 25 33 {ECO:0000244|PDB:1GAD}.
HELIX 38 46 {ECO:0000244|PDB:1GAD}.
TURN 49 51 {ECO:0000244|PDB:1GAD}.
STRAND 58 61 {ECO:0000244|PDB:1GAD}.
STRAND 64 67 {ECO:0000244|PDB:1GAD}.
STRAND 70 75 {ECO:0000244|PDB:1GAD}.
HELIX 80 83 {ECO:0000244|PDB:1GAD}.
HELIX 85 88 {ECO:0000244|PDB:1GAD}.
STRAND 91 95 {ECO:0000244|PDB:1GAD}.
STRAND 97 99 {ECO:0000244|PDB:1GAD}.
HELIX 103 106 {ECO:0000244|PDB:1GAD}.
HELIX 108 111 {ECO:0000244|PDB:1GAD}.
STRAND 115 121 {ECO:0000244|PDB:1GAD}.
STRAND 124 126 {ECO:0000244|PDB:1GAD}.
TURN 132 134 {ECO:0000244|PDB:1GAD}.
HELIX 136 138 {ECO:0000244|PDB:1GAD}.
STRAND 143 146 {ECO:0000244|PDB:1GAD}.
HELIX 150 166 {ECO:0000244|PDB:1GAD}.
STRAND 168 177 {ECO:0000244|PDB:1GAD}.
STRAND 183 187 {ECO:0000244|PDB:1GAD}.
HELIX 194 197 {ECO:0000244|PDB:1GAD}.
TURN 200 202 {ECO:0000244|PDB:1GAD}.
STRAND 205 208 {ECO:0000244|PDB:1GAD}.
TURN 211 214 {ECO:0000244|PDB:1GAD}.
HELIX 215 218 {ECO:0000244|PDB:1GAD}.
HELIX 220 222 {ECO:0000244|PDB:1GAD}.
STRAND 225 232 {ECO:0000244|PDB:1GAD}.
STRAND 239 249 {ECO:0000244|PDB:1GAD}.
HELIX 253 265 {ECO:0000244|PDB:1GAD}.
TURN 266 271 {ECO:0000244|PDB:1GAD}.
STRAND 272 275 {ECO:0000244|PDB:1GAD}.
HELIX 281 284 {ECO:0000244|PDB:1GAD}.
STRAND 289 294 {ECO:0000244|PDB:1GAD}.
TURN 295 297 {ECO:0000244|PDB:1GAD}.
STRAND 299 302 {ECO:0000244|PDB:1GAD}.
STRAND 305 312 {ECO:0000244|PDB:1GAD}.
HELIX 316 328 {ECO:0000244|PDB:1GAD}.
SEQUENCE 331 AA; 35532 MW; B3A460AA6D59E46D CRC64;
MTIKVGINGF GRIGRIVFRA AQKRSDIEIV AINDLLDADY MAYMLKYDST HGRFDGTVEV
KDGHLIVNGK KIRVTAERDP ANLKWDEVGV DVVAEATGLF LTDETARKHI TAGAKKVVMT
GPSKDNTPMF VKGANFDKYA GQDIVSNASC TTNCLAPLAK VINDNFGIIE GLMTTVHATT
ATQKTVDGPS HKDWRGGRGA SQNIIPSSTG AAKAVGKVLP ELNGKLTGMA FRVPTPNVSV
VDLTVRLEKA ATYEQIKAAV KAAAEGEMKG VLGYTEDDVV STDFNGEVCT SVFDAKAGIA
LNDNFVKLVS WYDNETGYSN KVLDLIAHIS K


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U1932r CLIA 38 kDa BFA-dependent ADP-ribosylation substrate,BARS-38,Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Rat,Rattus norvegicus 96T
U1932r CLIA kit 38 kDa BFA-dependent ADP-ribosylation substrate,BARS-38,Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Rat,Rattus norvegicus 96T
E1932r ELISA 38 kDa BFA-dependent ADP-ribosylation substrate,BARS-38,Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Rat,Rattus norvegicus 96T
E1932r ELISA kit 38 kDa BFA-dependent ADP-ribosylation substrate,BARS-38,Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Rat,Rattus norvegicus 96T
orb90368 Glyceraldehyde-3-PDH enzyme Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) is a purified enzyme. For research use only. 100
MC-993 Glyceraldehyde 3 phosphate Dehydrogenase (GAPDH) 1D4 100 uL
MC-993 Glyceraldehyde 3 phosphate Dehydrogenase (GAPDH) 100 uL
MC-993 Glyceraldehyde 3 phosphate Dehydrogenase (GAPDH) 100 uL
GWB-A7A45C GAPDH (glyceraldehyde-3-phosphate dehydrogenase)
5G4 Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) Antibodie 1 mg
MC-993 Glyceraldehyde 3 phosphate Dehydrogenase (GAPDH) Clone 1D4 100 uL
U1932p CLIA GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Pig,Sus scrofa 96T
E1932p ELISA kit GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Pig,Sus scrofa 96T
E1932p ELISA GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Pig,Sus scrofa 96T
U1932p CLIA kit GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Pig,Sus scrofa 96T
U1932m CLIA kit Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Mouse,Mus musculus,Peptidyl-cysteine S-nitrosylase GAPDH 96T
E1932b ELISA Bos taurus,Bovine,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH 96T
U1932m CLIA Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Mouse,Mus musculus,Peptidyl-cysteine S-nitrosylase GAPDH 96T
U1932b CLIA Bos taurus,Bovine,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH 96T
U1932b CLIA kit Bos taurus,Bovine,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH 96T
E1932m ELISA kit Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Mouse,Mus musculus,Peptidyl-cysteine S-nitrosylase GAPDH 96T
E1932m ELISA Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Mouse,Mus musculus,Peptidyl-cysteine S-nitrosylase GAPDH 96T
E1932b ELISA kit Bos taurus,Bovine,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH 96T
U1932Rb CLIA GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Oryctolagus cuniculus,Peptidyl-cysteine S-nitrosylase GAPDH,Rabbit 96T
E1932Rb ELISA kit GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Oryctolagus cuniculus,Peptidyl-cysteine S-nitrosylase GAPDH,Rabbit 96T


 

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