EzCatDB: D00010

DB codeD00010
CATH domainDomain 13.40.50.720
Domain 23.30.360.10Catalytic domain
E.C.1.1.1.49
CSA1dpg

CATH domainRelated DB codes (homologues)
3.30.360.10T00219,D00003,D00017,D00023,D00027,D00028,D00034,D00476
3.40.50.720S00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00324,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00012,D00017,D00018,D00023,D00027,D00028,D00031,D00032,D00033,D00034,D00035,D00037,D00048,D00071,D00476,D00481,D00482,D00490,D00492,D00494,D00545,D00601,D00603,D00604,D00605,D00615,D00845,D00857,D00858,M00161,M00171,M00210,T00002,T00010,T00011,T00015,T00227,T00247,T00408,T00414,D00827,D00262,D00274,D00275,M00035,T00109

Enzyme Name
Swiss-protKEGG

P11413P11411
Protein nameGlucose-6-phosphate 1-dehydrogenaseGlucose-6-phosphate 1-dehydrogenaseglucose-6-phosphate dehydrogenase
NADP-glucose-6-phosphate dehydrogenase
Zwischenferment
D-glucose 6-phosphate dehydrogenase
glucose 6-phosphate dehydrogenase (NADP)
NADP-dependent glucose 6-phosphate dehydrogenase
6-phosphoglucose dehydrogenase
Entner-Doudoroff enzyme
glucose-6-phosphate 1-dehydrogenase
G6PDH
GPD
SynonymsG6PD
EC 1.1.1.49
G6PD
EC 1.1.1.49

KEGG pathways
MAP codePathways
MAP00030Pentose phosphate pathway
MAP00480Glutathione metabolism

Swiss-prot:Accession NumberP11413P11411
Entry nameG6PD_HUMANG6PD_LEUME
ActivityD-glucose 6-phosphate + NADP(+) = D-glucono- 1,5-lactone 6-phosphate + NADPH.D-glucose 6-phosphate + NADP(+) = D-glucono- 1,5-lactone 6-phosphate + NADPH.
SubunitHomodimer or homotetramer.Homodimer.
Subcellular location

Cofactor



SubstratesProducts
KEGG-idC00092C00006C00003C01236C00005C00004C00080
CompoundD-Glucose 6-phosphateNADP+NAD+D-Glucono-1,5-lactone 6-phosphateNADPHNADHH+
Typecarbohydrate,phosphate group/phosphate ionamide group,amine group,nucleotideamide group,amine group,nucleotidecarbohydrate,phosphate group/phosphate ionamide group,amine group,nucleotideamide group,amine group,nucleotideothers
1dpgA01UnboundUnboundUnboundUnboundUnboundUnbound
1dpgB01UnboundUnboundUnboundUnboundUnboundUnbound
1e77A01UnboundUnboundUnboundUnboundUnboundUnbound
1e7mA01UnboundUnboundUnboundUnboundUnboundUnbound
1e7yA01UnboundUnboundUnboundUnboundAnalogue:NDPUnbound
1h93A01UnboundUnboundUnboundUnboundUnboundUnbound
1h94A01UnboundUnboundBound:NADUnboundUnboundUnbound
1h9aA01UnboundBound:NAPUnboundUnboundUnboundUnbound
1h9bA01UnboundUnboundUnboundUnboundUnboundUnbound
1qkiA01UnboundUnboundUnboundUnboundUnboundUnbound
1qkiB01UnboundUnboundUnboundUnboundUnboundUnbound
1qkiC01UnboundUnboundUnboundUnboundUnboundUnbound
1qkiD01UnboundUnboundUnboundUnboundUnboundUnbound
1qkiE01UnboundUnboundUnboundUnboundUnboundUnbound
1qkiF01UnboundUnboundUnboundUnboundUnboundUnbound
1qkiG01UnboundUnboundUnboundUnboundUnboundUnbound
1qkiH01UnboundUnboundUnboundUnboundUnboundUnbound
2dpgA01UnboundBound:NAPUnboundUnboundUnboundUnbound
1dpgA02UnboundUnboundUnboundUnboundUnboundUnbound
1dpgB02UnboundUnboundUnboundUnboundUnboundUnbound
1e77A02Bound:BG6UnboundUnboundUnboundUnboundUnbound
1e7mA02UnboundUnboundUnboundUnboundUnboundUnbound
1e7yA02Bound:BG6UnboundUnboundUnboundUnboundUnbound
1h93A02UnboundUnboundUnboundUnboundUnboundUnbound
1h94A02UnboundUnboundUnboundUnboundUnboundUnbound
1h9aA02UnboundUnboundUnboundUnboundUnboundUnbound
1h9bA02UnboundUnboundUnboundUnboundUnboundUnbound
1qkiA02UnboundBound:NAPUnboundUnboundUnboundUnbound
1qkiB02UnboundBound:NAPUnboundUnboundUnboundUnbound
1qkiC02UnboundBound:NAPUnboundUnboundUnboundUnbound
1qkiD02UnboundBound:NAPUnboundUnboundUnboundUnbound
1qkiE02UnboundBound:NAPUnboundUnboundUnboundUnbound
1qkiF02UnboundBound:NAPUnboundUnboundUnboundUnbound
1qkiG02UnboundBound:NAPUnboundUnboundUnboundUnbound
1qkiH02UnboundBound:NAPUnboundUnboundUnboundUnbound
2dpgA02UnboundUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
Swiss-prot;P11411, literature [13], [15], [20]
pdbCatalytic residuescomment
1dpgA01
mutant S61C
1dpgB01
mutant S61C
1e77A01

1e7mA01

1e7yA01

1h93A01

1h94A01

1h9aA01

1h9bA01

1qkiA01

1qkiB01

1qkiC01

1qkiD01

1qkiE01

1qkiF01

1qkiG01

1qkiH01

2dpgA01

1dpgA02ASP 177;HIS 240

1dpgB02ASP 177;HIS 240

1e77A02ASP 177;HIS 240
mutant Q365C
1e7mA02       ;HIS 240
mutant D177N
1e7yA02       ;HIS 240
mutant D177N
1h93A02ASP 177;HIS 240
mutant S215C
1h94A02ASP 177;HIS 240
mutant S215C
1h9aA02ASP 177;HIS 240
mutant Q365C
1h9bA02ASP 177;HIS 240
mutant Q365C
1qkiA02ASP 200;HIS 263
variant R459L
1qkiB02ASP 200;HIS 263
variant R459L
1qkiC02ASP 200;HIS 263
variant R459L
1qkiD02ASP 200;HIS 263
variant R459L
1qkiE02ASP 200;HIS 263
variant R459L
1qkiF02ASP 200;HIS 263
variant R459L
1qkiG02ASP 200;HIS 263
variant R459L
1qkiH02ASP 200;HIS 263
variant R459L
2dpgA02ASP 177;       
mutant H240N

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.131-133
[11]p.1081-1082
[12]

[13]Scheme 1, p.2765
[15]Scheme 1, p.15010
[16]p.15019-15021
[20]p.646-647
[21]


references
[1]
PubMed ID367106
JournalAdv Enzymol Relat Areas Mol Biol
Year1979
Volume48
Pages97-192
AuthorsLevy HR
TitleGlucose-6-phosphate dehydrogenases.
[2]
PubMed ID6847197
JournalArch Biochem Biophys
Year1983
Volume222
Pages473-88
AuthorsLevy HR, Christoff M, Ingulli J, Ho EM
TitleGlucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: revised kinetic mechanism and kinetics of ATP inhibition.
[3]
PubMed ID6655694
JournalJ Mol Biol
Year1983
Volume171
Pages233-6
AuthorsAmmon HL, Murphy KC, Bhattacharjee SK, Szepesi B, Hansen RJ
TitlePreliminary crystallographic study of glucose-6-phosphate dehydrogenase from rat liver.
[4]
PubMed ID6696439
JournalArch Biochem Biophys
Year1984
Volume228
Pages415-24
AuthorsViola RE
TitleKinetic studies of the reactions catalyzed by glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: pH variation of kinetic parameters.
[5]
PubMed ID3720867
JournalExp Eye Res
Year1986
Volume42
Pages489-96
AuthorsDovrat A, Scharf J, Eisenbach L, Gershon D
TitleG6PD molecules devoid of catalytic activity are present in the nucleus of the rat lens.
[6]
PubMed ID3581436
JournalCell Biochem Funct
Year1987
Volume5
Pages79-95
AuthorsRosemeyer MA
TitleThe biochemistry of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase.
[7]
PubMed ID3072957
JournalBiochem Int
Year1988
Volume17
Pages1099-106
AuthorsKim YS, Kim YI, Byun HS
TitleInactivation of Saccharomyces cerevisiae glucose-6-phosphate dehydrogenase by diethylpyrocarbonate.
[8]
PubMed ID2590166
JournalBiochem J
Year1989
Volume262
Pages795-800
AuthorsAon MA, Cortassa S, Hervagault JF, Thomas D
TitlepH-induced bistable dynamic behaviour in the reaction catalysed by glucose-6-phosphate dehydrogenase and conformational hysteresis of the enzyme.
[9]
PubMed ID1304341
JournalProtein Sci
Year1992
Volume1
Pages329-34
AuthorsLee WT, Levy HR
TitleLysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction.
[10]
PubMed ID8495203
JournalProtein Sci
Year1993
Volume2
Pages859-62
AuthorsAdams MJ, Basak AK, Gover S, Rowland P, Levy HR
TitleSite-directed mutagenesis to facilitate X-ray structural studies of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase.
[11]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed ID7881907
JournalStructure
Year1994
Volume2
Pages1073-87
AuthorsRowland P, Basak AK, Gover S, Levy HR, Adams MJ
TitleThe three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 A resolution.
Related PDB1dpg
Related Swiss-protP11411
[12]
PubMed ID7789519
JournalFEBS Lett
Year1995
Volume366
Pages61-4
AuthorsBautista JM, Mason PJ, Luzzatto L
TitleHuman glucose-6-phosphate dehydrogenase. Lysine 205 is dispensable for substrate binding but essential for catalysis.
[13]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ASN-240, AND MUTAGENESIS OF ASP-177; HIS-178 AND HIS-240.
PubMed ID9485426
JournalBiochemistry
Year1998
Volume37
Pages2759-67
AuthorsCosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR
TitleOn the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase.
Related PDB2dpg
Related Swiss-protP11411
[14]
PubMed ID10089300
JournalActa Crystallogr D Biol Crystallogr
Year1999
Volume55
Pages826-34
AuthorsAu SW, Naylor CE, Gover S, Vandeputte-Rutten L, Scopes DA, Mason PJ, Luzzatto L, Lam VM, Adams MJ
TitleSolution of the structure of tetrameric human glucose 6-phosphate dehydrogenase by molecular replacement.
[15]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS ASN-177 AND CYS-365 IN COMPLEX WITH NAD; NADP AND SUBSTRATE.
PubMed ID11106478
JournalBiochemistry
Year2000
Volume39
Pages15002-11
AuthorsCosgrove MS, Gover S, Naylor CE, Vandeputte-Rutten L, Adams MJ, Levy HR
TitleAn 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.
Related PDB1e77,1e7m,1e7y
Related Swiss-protP11411
[16]
PubMed ID11106479
JournalBiochemistry
Year2000
Volume39
Pages15012-21
AuthorsVought V, Ciccone T, Davino MH, Fairbairn L, Lin Y, Cosgrove MS, Adams MJ, Levy HR
TitleDelineation of the roles of amino acids involved in the catalytic functions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase.
[17]
PubMed ID10734064
JournalJ Biol Chem
Year2000
Volume275
Pages9256-62
AuthorsGomez-Gallego F, Garrido-Pertierra A, Bautista JM
TitleStructural defects underlying protein dysfunction in human glucose-6-phosphate dehydrogenase A(-) deficiency.
[18]
PubMed ID10959850
JournalJ Org Chem
Year2000
Volume65
Pages4498-508
AuthorsBerkowitz DB, Bose M, Pfannenstiel TJ, Doukov T
Titlealpha-fluorinated phosphonates as substrate mimics for glucose 6-phosphate dehydrogenase: the CHF stereochemistry matters.
[19]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF VARIANT CANTON IN COMPLEX WITH NADP, AND HOMOTETRAMERIZATION.
PubMed ID10745013
JournalStructure Fold Des
Year2000
Volume8
Pages293-303
AuthorsAu SW, Gover S, Lam VM, Adams MJ
TitleHuman glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency.
Related PDB1qki
Related Swiss-protP11413
[20]
CommentsX-ray crystallography
PubMed ID11320304
JournalActa Crystallogr D Biol Crystallogr
Year2001
Volume57
Pages635-48
AuthorsNaylor CE, Gover S, Basak AK, Cosgrove MS, Levy HR, Adams MJ
TitleNADP+ 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.
Related PDB1h93,1h94,1h9a,1h9b
[21]
PubMed ID12033926
JournalBiochemistry
Year2002
Volume41
Pages6939-45
AuthorsCosgrove MS, Loh SN, Ha JH, Levy HR
TitleThe catalytic mechanism of glucose 6-phosphate dehydrogenases: assignment and 1H NMR spectroscopy pH titration of the catalytic histidine residue in the 109 kDa Leuconostoc mesenteroides enzyme.

comments
For this enzyme, glucose-6-phosphate 1-dehydrogenase, NAD(P)+/NAD(P)H, which is involved in catalysis, should be bound to the N-terminal domain, NADP binding domain. However, in the case of the human enzyme, it has another binding site for NAD(P)+/NAD(P)H, which is responsible for structural stability, in the C-terminal doman (see [19]). The sturcture of the human counterpart, 1qki (PDB), has got the structural NADP+ molecules.

createdupdated
2004-03-242009-02-26
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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