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Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.363) (Glucose-6-phosphate dehydrogenase (NAD(P)( )))

 G6PD_LEUME              Reviewed;         486 AA.
P11411;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
05-DEC-2018, entry version 136.
RecName: Full=Glucose-6-phosphate 1-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00966};
Short=G6PD {ECO:0000255|HAMAP-Rule:MF_00966};
EC=1.1.1.363 {ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:11106479, ECO:0000269|PubMed:1304341, ECO:0000269|PubMed:4396688, ECO:0000269|PubMed:9485426};
AltName: Full=Glucose-6-phosphate dehydrogenase (NAD(P)(+)) {ECO:0000305};
Name=zwf {ECO:0000255|HAMAP-Rule:MF_00966};
Leuconostoc mesenteroides.
Bacteria; Firmicutes; Bacilli; Lactobacillales; Leuconostocaceae;
Leuconostoc.
NCBI_TaxID=1245;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 12291;
PubMed=2071589;
Lee W.T., Flynn T.G., Lyons C., Levy H.R.;
"Cloning of the gene and amino acid sequence for glucose 6-phosphate
dehydrogenase from Leuconostoc mesenteroides.";
J. Biol. Chem. 266:13028-13034(1991).
[2]
PROTEIN SEQUENCE OF 147-188.
PubMed=3100332; DOI=10.1016/0014-5793(87)81445-X;
Bhadbhade M.M., Adams M.J., Flynn T.G., Levy H.R.;
"Sequence identity between a lysine-containing peptide from
Leuconostoc mesenteroides glucose-6-phosphate dehydrogenase and an
active site peptide from human erythrocyte glucose-6-phosphate
dehydrogenase.";
FEBS Lett. 211:243-246(1987).
[3]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=4396688;
Olive C., Geroch M.E., Levy H.R.;
"Glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides.
Kinetic studies.";
J. Biol. Chem. 246:2047-2057(1971).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-22.
PubMed=1304341; DOI=10.1002/pro.5560010304;
Lee W.T., Levy H.R.;
"Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate
dehydrogenase participates in substrate binding through charge-charge
interaction.";
Protein Sci. 1:329-334(1992).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-15; LYS-22;
ARG-47; GLN-48; PRO-150; TYR-180; LYS-183; LYS-344; ASP-375 AND
TYR-416.
PubMed=11106479; DOI=10.1021/bi0014610;
Vought V., Ciccone T., Davino M.H., Fairbairn L., Lin Y.,
Cosgrove M.S., Adams M.J., Levy H.R.;
"Delineation of the roles of amino acids involved in the catalytic
functions of Leuconostoc mesenteroides glucose 6-phosphate
dehydrogenase.";
Biochemistry 39:15012-15021(2000).
[6] {ECO:0000244|PDB:1DPG}
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=7881907; DOI=10.1016/S0969-2126(94)00110-3;
Rowland P., Basak A.K., Gover S., Levy H.R., Adams M.J.;
"The three-dimensional structure of glucose 6-phosphate dehydrogenase
from Leuconostoc mesenteroides refined at 2.0-A resolution.";
Structure 2:1073-1087(1994).
[7] {ECO:0000244|PDB:2DPG}
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ASN-241 IN COMPLEX
WITH NADP, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF ASP-178; HIS-179 AND
HIS-241.
PubMed=9485426; DOI=10.1021/bi972069y;
Cosgrove M.S., Naylor C., Paludan S., Adams M.J., Levy H.R.;
"On the mechanism of the reaction catalyzed by glucose 6-phosphate
dehydrogenase.";
Biochemistry 37:2759-2767(1998).
[8] {ECO:0000244|PDB:1E77, ECO:0000244|PDB:1E7M, ECO:0000244|PDB:1E7Y}
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS ASN-178 AND CYS-366
IN COMPLEXES WITH NAD; NADP AND GLUCOSE 6-PHOSPHATE, CATALYTIC
ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=11106478; DOI=10.1021/bi0014608;
Cosgrove M.S., Gover S., Naylor C.E., Vandeputte-Rutten L.,
Adams M.J., Levy H.R.;
"An examination of the role of Asp-177 in the His-Asp catalytic dyad
of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: X-ray
structure and pH dependence of kinetic parameters of the D177N mutant
enzyme.";
Biochemistry 39:15002-15011(2000).
[9] {ECO:0000244|PDB:1H93, ECO:0000244|PDB:1H94, ECO:0000244|PDB:1H9A, ECO:0000244|PDB:1H9B}
X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS) IN COMPLEXES WITH NAD AND NADP.
PubMed=11320304; DOI=10.1107/S0907444901003420;
Naylor C.E., Gover S., Basak A.K., Cosgrove M.S., Levy H.R.,
Adams M.J.;
"NADP+ and NAD+ binding to the dual coenzyme specific enzyme
Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase: different
interdomain hinge angles are seen in different binary and ternary
complexes.";
Acta Crystallogr. D 57:635-648(2001).
-!- FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-
phosphogluconolactone. Can utilize either NADP(+) or NAD(+).
{ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:11106479,
ECO:0000269|PubMed:1304341, ECO:0000269|PubMed:4396688,
ECO:0000269|PubMed:9485426}.
-!- CATALYTIC ACTIVITY:
Reaction=D-glucose 6-phosphate + NAD(+) = 6-phospho-D-glucono-1,5-
lactone + H(+) + NADH; Xref=Rhea:RHEA:38215, ChEBI:CHEBI:15378,
ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57955,
ChEBI:CHEBI:61548; EC=1.1.1.363;
Evidence={ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:11106479, ECO:0000269|PubMed:1304341,
ECO:0000269|PubMed:4396688, ECO:0000269|PubMed:9485426};
-!- CATALYTIC ACTIVITY:
Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-
1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841,
ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955,
ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.363;
Evidence={ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:11106479, ECO:0000269|PubMed:1304341,
ECO:0000269|PubMed:4396688, ECO:0000269|PubMed:9485426};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=114 uM for glucose 6-phosphate (with NADP)
{ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:9485426};
KM=69 uM for glucose 6-phosphate (with NAD)
{ECO:0000269|PubMed:11106478, ECO:0000269|PubMed:9485426};
KM=8.0 uM for NADP {ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:9485426};
KM=160 uM for NAD {ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:9485426};
pH dependence:
Optimum pH is 5.4-8.9. {ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:9485426};
-!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage):
step 1/3. {ECO:0000255|HAMAP-Rule:MF_00966}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:9485426}.
-!- SIMILARITY: Belongs to the glucose-6-phosphate dehydrogenase
family. {ECO:0000255|HAMAP-Rule:MF_00966}.
-!- WEB RESOURCE: Name=Worthington enzyme manual;
URL="http://www.worthington-biochem.com/ZF/";
-----------------------------------------------------------------------
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EMBL; M64446; AAA25265.1; -; Genomic_DNA.
PIR; A39864; A39864.
PDB; 1DPG; X-ray; 2.00 A; A/B=2-486.
PDB; 1E77; X-ray; 2.69 A; A=2-486.
PDB; 1E7M; X-ray; 2.54 A; A=2-486.
PDB; 1E7Y; X-ray; 2.48 A; A=2-486.
PDB; 1H93; X-ray; 2.20 A; A=2-486.
PDB; 1H94; X-ray; 2.50 A; A=2-486.
PDB; 1H9A; X-ray; 2.16 A; A=2-486.
PDB; 1H9B; X-ray; 2.40 A; A=2-486.
PDB; 2DPG; X-ray; 2.50 A; A=2-486.
PDBsum; 1DPG; -.
PDBsum; 1E77; -.
PDBsum; 1E7M; -.
PDBsum; 1E7Y; -.
PDBsum; 1H93; -.
PDBsum; 1H94; -.
PDBsum; 1H9A; -.
PDBsum; 1H9B; -.
PDBsum; 2DPG; -.
ProteinModelPortal; P11411; -.
SMR; P11411; -.
BindingDB; P11411; -.
ChEMBL; CHEMBL1741173; -.
DrugBank; DB03461; 2'-Monophosphoadenosine 5'-Diphosphoribose.
DrugBank; DB04122; beta-D-glucose 6-phosphate.
DrugBank; DB02338; Nadph Dihydro-Nicotinamide-Adenine-Dinucleotidephosphate.
PRIDE; P11411; -.
KEGG; ag:AAA25265; -.
KO; K00036; -.
BioCyc; MetaCyc:MONOMER-13060; -.
BRENDA; 1.1.1.363; 839.
SABIO-RK; P11411; -.
UniPathway; UPA00115; UER00408.
EvolutionaryTrace; P11411; -.
GO; GO:0004345; F:glucose-6-phosphate dehydrogenase activity; IEA:UniProtKB-UniRule.
GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
HAMAP; MF_00966; G6PD; 1.
InterPro; IPR001282; G6P_DH.
InterPro; IPR019796; G6P_DH_AS.
InterPro; IPR022675; G6P_DH_C.
InterPro; IPR022674; G6P_DH_NAD-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR23429; PTHR23429; 1.
Pfam; PF02781; G6PD_C; 1.
Pfam; PF00479; G6PD_N; 1.
PIRSF; PIRSF000110; G6PD; 1.
PRINTS; PR00079; G6PDHDRGNASE.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00871; zwf; 1.
PROSITE; PS00069; G6P_DEHYDROGENASE; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism; Direct protein sequencing;
Glucose metabolism; NAD; NADP; Oxidoreductase.
INIT_MET 1 1 Removed.
CHAIN 2 486 Glucose-6-phosphate 1-dehydrogenase.
/FTId=PRO_0000068125.
NP_BIND 13 20 NADP. {ECO:0000255|HAMAP-Rule:MF_00966,
ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:11320304,
ECO:0000269|PubMed:9485426}.
NP_BIND 86 87 NADP. {ECO:0000255|HAMAP-Rule:MF_00966,
ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:11320304,
ECO:0000269|PubMed:9485426}.
ACT_SITE 241 241 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_00966,
ECO:0000269|PubMed:9485426}.
BINDING 47 47 NADP. {ECO:0000255|HAMAP-Rule:MF_00966,
ECO:0000269|PubMed:11106478,
ECO:0000269|PubMed:11320304,
ECO:0000269|PubMed:9485426}.
BINDING 149 149 NADP. {ECO:0000255|HAMAP-Rule:MF_00966,
ECO:0000269|PubMed:11320304}.
BINDING 179 179 Substrate. {ECO:0000305|PubMed:11106478}.
BINDING 183 183 Substrate. {ECO:0000305|PubMed:11106478}.
BINDING 217 217 Substrate. {ECO:0000305|PubMed:11106478}.
BINDING 236 236 Substrate. {ECO:0000305|PubMed:11106478}.
BINDING 339 339 Substrate. {ECO:0000305|PubMed:11106478}.
BINDING 344 344 Substrate. {ECO:0000305|PubMed:11106478}.
MUTAGEN 15 15 T->A: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 15 15 T->S: Decreases catalytic efficiency
toward glucose 6-phosphate (with NAD).
{ECO:0000269|PubMed:11106479}.
MUTAGEN 22 22 K->E: Almost loss of activity.
{ECO:0000269|PubMed:11106479,
ECO:0000269|PubMed:1304341}.
MUTAGEN 22 22 K->Q: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479,
ECO:0000269|PubMed:1304341}.
MUTAGEN 22 22 K->R: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479,
ECO:0000269|PubMed:1304341}.
MUTAGEN 47 47 R->A: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 48 48 Q->A,E: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 150 150 P->G,V: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 178 178 D->N: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:9485426}.
MUTAGEN 179 179 H->N: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:9485426}.
MUTAGEN 180 180 Y->F: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 183 183 K->Q,R: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 241 241 H->N: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:9485426}.
MUTAGEN 344 344 K->Q,R: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 375 375 D->Q: Strongly decreases catalytic
efficiency toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
MUTAGEN 416 416 Y->F: Decreases catalytic efficiency
toward glucose 6-phosphate.
{ECO:0000269|PubMed:11106479}.
CONFLICT 154 156 SYD -> HYI (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 165 165 L -> F (in Ref. 2; AA sequence).
{ECO:0000305}.
STRAND 7 12 {ECO:0000244|PDB:1DPG}.
TURN 13 15 {ECO:0000244|PDB:1DPG}.
HELIX 17 21 {ECO:0000244|PDB:1DPG}.
HELIX 23 32 {ECO:0000244|PDB:1DPG}.
STRAND 38 48 {ECO:0000244|PDB:1DPG}.
HELIX 52 63 {ECO:0000244|PDB:1DPG}.
HELIX 64 66 {ECO:0000244|PDB:1DPG}.
HELIX 70 77 {ECO:0000244|PDB:1DPG}.
STRAND 80 84 {ECO:0000244|PDB:1DPG}.
HELIX 92 106 {ECO:0000244|PDB:1DPG}.
STRAND 113 117 {ECO:0000244|PDB:1DPG}.
HELIX 121 123 {ECO:0000244|PDB:1DPG}.
HELIX 124 133 {ECO:0000244|PDB:1DPG}.
STRAND 139 141 {ECO:0000244|PDB:1DPG}.
STRAND 143 147 {ECO:0000244|PDB:1DPG}.
HELIX 155 165 {ECO:0000244|PDB:1DPG}.
TURN 166 168 {ECO:0000244|PDB:1DPG}.
HELIX 171 173 {ECO:0000244|PDB:1DPG}.
STRAND 174 176 {ECO:0000244|PDB:1DPG}.
HELIX 179 182 {ECO:0000244|PDB:1DPG}.
HELIX 184 188 {ECO:0000244|PDB:1DPG}.
HELIX 189 194 {ECO:0000244|PDB:1DPG}.
HELIX 197 200 {ECO:0000244|PDB:1DPG}.
TURN 205 207 {ECO:0000244|PDB:1DPG}.
STRAND 208 216 {ECO:0000244|PDB:1DPG}.
HELIX 222 224 {ECO:0000244|PDB:1H9A}.
HELIX 225 236 {ECO:0000244|PDB:1DPG}.
TURN 237 240 {ECO:0000244|PDB:1DPG}.
HELIX 241 250 {ECO:0000244|PDB:1DPG}.
STRAND 255 258 {ECO:0000244|PDB:1DPG}.
HELIX 259 270 {ECO:0000244|PDB:1DPG}.
HELIX 278 284 {ECO:0000244|PDB:1DPG}.
STRAND 285 290 {ECO:0000244|PDB:1DPG}.
STRAND 294 298 {ECO:0000244|PDB:1H9A}.
HELIX 301 303 {ECO:0000244|PDB:1DPG}.
STRAND 315 321 {ECO:0000244|PDB:1DPG}.
HELIX 326 328 {ECO:0000244|PDB:1DPG}.
STRAND 333 343 {ECO:0000244|PDB:1DPG}.
STRAND 345 352 {ECO:0000244|PDB:1DPG}.
STRAND 361 363 {ECO:0000244|PDB:1DPG}.
STRAND 369 377 {ECO:0000244|PDB:1DPG}.
STRAND 379 387 {ECO:0000244|PDB:1DPG}.
STRAND 389 392 {ECO:0000244|PDB:1DPG}.
STRAND 395 403 {ECO:0000244|PDB:1DPG}.
HELIX 406 411 {ECO:0000244|PDB:1DPG}.
HELIX 415 425 {ECO:0000244|PDB:1DPG}.
HELIX 428 430 {ECO:0000244|PDB:1H94}.
HELIX 434 452 {ECO:0000244|PDB:1DPG}.
STRAND 459 461 {ECO:0000244|PDB:1DPG}.
STRAND 465 467 {ECO:0000244|PDB:1DPG}.
HELIX 469 476 {ECO:0000244|PDB:1DPG}.
TURN 477 479 {ECO:0000244|PDB:1DPG}.
SEQUENCE 486 AA; 54441 MW; AA43433F83ED091D CRC64;
MVSEIKTLVT FFGGTGDLAK RKLYPSVFNL YKKGYLQKHF AIVGTARQAL NDDEFKQLVR
DSIKDFTDDQ AQAEAFIEHF SYRAHDVTDA ASYAVLKEAI EEAADKFDID GNRIFYMSVA
PRFFGTIAKY LKSEGLLADT GYNRLMIEKP FGTSYDTAAE LQNDLENAFD DNQLFRIDHY
LGKEMVQNIA ALRFGNPIFD AAWNKDYIKN VQVTLSEVLG VEERAGYYDT AGALLDMIQN
HTMQIVGWLA MEKPESFTDK DIRAAKNAAF NALKIYDEAE VNKYFVRAQY GAGDSADFKP
YLEELDVPAD SKNNTFIAGE LQFDLPRWEG VPFYVRSGKR LAAKQTRVDI VFKAGTFNFG
SEQEAQEAVL SIIIDPKGAI ELKLNAKSVE DAFNTRTIDL GWTVSDEDKK NTPEPYERMI
HDTMNGDGSN FADWNGVSIA WKFVDAISAV YTADKAPLET YKSGSMGPEA SDKLLAANGD
AWVFKG


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Pathways :
WP253: Glycolysis
WP312: Pentose Phosphate Pathway
WP1493: Carbon assimilation C4 pathway
WP1657: Glycerolipid metabolism
WP260: Glucose-1-phosphate metabolism
WP575: Anaerobic respiration
WP1028: Pentose Phosphate Pathway
WP1147: Pentose Phosphate Pathway
WP122: Pentose Phosphate Pathway
WP1231: Pentose Phosphate Pathway
WP134: Pentose Phosphate Pathway
WP282: Pentose Phosphate Pathway
WP797: Pentose Phosphate Pathway
WP911: Pentose Phosphate Pathway
WP109: UDP-Glucose Conversion
WP1566: Citrate cycle (TCA cycle)
WP1567: Glycolysis and Gluconeogenesis
WP1581: Histidine metabolism
WP1612: 1,2-Dichloroethane degradation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1615: 3-Chloroacrylic acid degradation
WP1621: Arginine and proline metabolism
WP1622: Ascorbate and aldarate metabolism
WP1626: Benzoate degradation via CoA ligation
WP1627: Benzoate degradation via hydroxylation

Related Genes :
[zwf] Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.363) (Glucose-6-phosphate dehydrogenase (NAD(P)(+)))
[G6PD] Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49)
[zwf b1852 JW1841] Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49) [Cleaved into: Extracellular death factor (EDF)]
[ZWF1 MET19 YNL241C N1110] Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49)
[zwf PA3183] Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.363) (Glucose-6-phosphate dehydrogenase (NAD(P)(+)))
[fgd fgd1 MSMEG_0777 MSMEI_0761] F420-dependent glucose-6-phosphate dehydrogenase (FGD) (G6PD) (EC 1.1.98.2)
[fgd1 fgd Rv0407] F420-dependent glucose-6-phosphate dehydrogenase (FGD) (FGD1) (G6PD) (EC 1.1.98.2)
[zwf GOX0145] Glucose-6-phosphate 1-dehydrogenase (G6PD) (G6PDH) (EC 1.1.1.49)
[gdh] Glucose 1-dehydrogenase (GDH) (GlcDH) (EC 1.1.1.47) (Aldose 1-dehydrogenase [NAD(P)(+)]) (EC 1.1.1.359) (Galactose 1-dehydrogenase) (EC 1.1.1.120) (EC 1.1.1.48)
[zwf MSMEG_0314 MSMEI_0307] Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49)
[gdh TTX_0329] Glucose 1-dehydrogenase (GDH) (GlcDH) (EC 1.1.1.47)
[gapN] NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.90) (Glyceraldehyde phosphate dehydrogenase (NAD(P))) (GAPN)
[egsA APE_0519.1] Glycerol-1-phosphate dehydrogenase [NAD(P)+] (G1P dehydrogenase) (G1PDH) (Gro1PDH) (EC 1.1.1.261) (Enantiomeric glycerophosphate synthase) (sn-glycerol-1-phosphate dehydrogenase)
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[rep 1a-1b] Replicase polyprotein 1ab (ORF1ab polyprotein) [Cleaved into: Nsp1-alpha papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-alpha); Nsp1-beta papain-like cysteine proteinase (EC 3.4.22.-) (PCP1-beta); Nsp2 cysteine proteinase (EC 3.4.22.-) (CP2) (CP); Non-structural protein 3 (Nsp3); 3C-like serine proteinase (3CLSP) (EC 3.4.21.-) (Nsp4); Non-structural protein 5-6-7 (Nsp5-6-7); Non-structural protein 5 (Nsp5); Non-structural protein 6 (Nsp6); Non-structural protein 7-alpha (Nsp7-alpha); Non-structural protein 7-beta (Nsp7-beta); Non-structural protein 8 (Nsp8); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Nsp9); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Nsp10); Non-structural protein 11 (Nsp11); Non-structural protein 12 (Nsp12)]
[TPS1 BYP1 CIF1 FDP1 GGS1 GLC6 TSS1 YBR126C YBR0922] Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit (EC 2.4.1.15) (General glucose sensor subunit 1) (Glycogen metabolism control protein GLC6) (Trehalose synthase complex catalytic subunit TPS1) (Trehalose-6-phosphate synthase) (UDP-glucose-glucosephosphate glucosyltransferase)
[Sirt2 Sir2l2] NAD-dependent protein deacetylase sirtuin-2 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2) (mSIR2L2)
[Gpi Gpi1] Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Autocrine motility factor) (AMF) (Neuroleukin) (NLK) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI)
[rfbA rmlA rmlA1 b2039 JW2024] Glucose-1-phosphate thymidylyltransferase 1 (G1P-TT 1) (EC 2.7.7.24) (dTDP-glucose pyrophosphorylase 1) (dTDP-glucose synthase 1)
[gdh2 gdhA PTO1070] Glucose/galactose 1-dehydrogenase (EC 1.1.1.360) (Galactose 1-dehydrogenase [NADP(+)]) (Glucose 1-dehydrogenase 2) (GDH 2) (GlcDH 2)
[RHM1 ROL1 At1g78570 T30F21.10] Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1 (Protein REPRESSOR OF LRX1 1) (Rhamnose biosynthetic enzyme 1) (AtRHM1) [Includes: UDP-glucose 4,6-dehydratase (EC 4.2.1.76); UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase (EC 1.1.1.-) (EC 5.1.3.-)]
[RHM2 MUM4 At1g53500 F22G10.13 T3F20.18] Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM2 (NDP-rhamnose synthase) (Protein MUCILAGE-MODIFIED 4) (Protein RHAMNOSE BIOSYNTHESIS 2) (Rhamnose biosynthetic enzyme 2) (AtRHM2) (UDP-L-rhamnose synthase MUM4) [Includes: UDP-glucose 4,6-dehydratase (EC 4.2.1.76); UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase (EC 1.1.1.-) (EC 5.1.3.-)]
[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
[gdh Ta0897] Glucose 1-dehydrogenase (GDH) (GlcDH) (EC 1.1.1.47) (Galactose 1-dehydrogenase) (EC 1.1.1.120) (EC 1.1.1.48)
[G6pc2 Igrp] Glucose-6-phosphatase 2 (G-6-Pase 2) (G6Pase 2) (EC 3.1.3.9) (Islet-specific glucose-6-phosphatase catalytic subunit-related protein)
[zwf OR214_03473] Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49)
[zwf OR16_17906] Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49)
[zwf OR16_03567] Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49)
[zwf OR221_1156] Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49)
[egsA MTH_610] Glycerol-1-phosphate dehydrogenase [NAD(P)+] (G1P dehydrogenase) (G1PDH) (EC 1.1.1.261) (Enantiomeric glycerophosphate synthase) (sn-glycerol-1-phosphate dehydrogenase)

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