DB code: D00010

CATH domain 3.40.50.720 : Rossmann fold
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 Catalytic domain
E.C. 1.1.1.49
CSA 1dpg
M-CSA 1dpg
MACiE

CATH domain Related DB codes (homologues)
3.40.50.720 : Rossmann fold S00543 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
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 T00219 D00003 D00017 D00023 D00027 D00028 D00034 D00476

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P11413 Glucose-6-phosphate 1-dehydrogenase
G6PD
EC 1.1.1.49
NP_000393.4 (Protein)
NM_000402.3 (DNA/RNA sequence)
NP_001035810.1 (Protein)
NM_001042351.1 (DNA/RNA sequence)
PF02781 (G6PD_C)
PF00479 (G6PD_N)
[Graphical View]
P11411 Glucose-6-phosphate 1-dehydrogenase
G6PD
EC 1.1.1.49
PF02781 (G6PD_C)
PF00479 (G6PD_N)
[Graphical View]

KEGG enzyme name
glucose-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

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P11411 G6PD_LEUME D-glucose 6-phosphate + NADP(+) = D-glucono- 1,5-lactone 6-phosphate + NADPH. Homodimer.
P11413 G6PD_HUMAN D-glucose 6-phosphate + NADP(+) = D-glucono- 1,5-lactone 6-phosphate + NADPH. Homodimer or homotetramer.

KEGG Pathways
Map code Pathways E.C.
MAP00480 Glutathione metabolism
MAP00030 Pentose phosphate pathway

Compound table
Substrates Products Intermediates
KEGG-id C00092 C00006 C00003 C01236 C00005 C00004 C00080
E.C.
Compound D-Glucose 6-phosphate NADP+ NAD+ D-Glucono-1,5-lactone 6-phosphate NADPH NADH H+
Type carbohydrate,phosphate group/phosphate ion amide group,amine group,nucleotide amide group,amine group,nucleotide carbohydrate,phosphate group/phosphate ion amide group,amine group,nucleotide amide group,amine group,nucleotide others
ChEBI 4170
18009
15846
16938
16474
16908
15378
PubChem 5958
5886
5893
439452
5884
439153
1038
1dpgA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1dpgB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1e77A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1e7mA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1e7yA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Analogue:NDP Unbound
1h93A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1h94A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Bound:NAD Unbound Unbound Unbound
1h9aA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound
1h9bA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qkiA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qkiB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qkiC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qkiD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qkiE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qkiF01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qkiG01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qkiH01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
2dpgA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound
1dpgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1dpgB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1e77A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:BG6 Unbound Unbound Unbound Unbound Unbound
1e7mA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1e7yA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Bound:BG6 Unbound Unbound Unbound Unbound Unbound
1h93A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1h94A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1h9aA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1h9bA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound
1qkiA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound
1qkiB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound
1qkiC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound
1qkiD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound
1qkiE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound
1qkiF02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound
1qkiG02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound
1qkiH02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Bound:NAP Unbound Unbound Unbound Unbound
2dpgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;P11411, literature [13], [15], [20]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dpgA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant S61C
1dpgB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain mutant S61C
1e77A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1e7mA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1e7yA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1h93A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1h94A01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1h9aA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1h9bA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qkiA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qkiB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qkiC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qkiD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qkiE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qkiF01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qkiG01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1qkiH01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2dpgA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1dpgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 177;HIS 240
1dpgB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 177;HIS 240
1e77A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 177;HIS 240 mutant Q365C
1e7mA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 240 mutant D177N
1e7yA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;HIS 240 mutant D177N
1h93A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 177;HIS 240 mutant S215C
1h94A02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 177;HIS 240 mutant S215C
1h9aA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 177;HIS 240 mutant Q365C
1h9bA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 177;HIS 240 mutant Q365C
1qkiA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 200;HIS 263 variant R459L
1qkiB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 200;HIS 263 variant R459L
1qkiC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 200;HIS 263 variant R459L
1qkiD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 200;HIS 263 variant R459L
1qkiE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 200;HIS 263 variant R459L
1qkiF02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 200;HIS 263 variant R459L
1qkiG02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 200;HIS 263 variant R459L
1qkiH02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 200;HIS 263 variant R459L
2dpgA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 177; mutant H240N

References for Catalytic Mechanism
References Sections No. 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]
Resource
Comments
Medline ID
PubMed ID 367106
Journal Adv Enzymol Relat Areas Mol Biol
Year 1979
Volume 48
Pages 97-192
Authors Levy HR
Title Glucose-6-phosphate dehydrogenases.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 6847197
Journal Arch Biochem Biophys
Year 1983
Volume 222
Pages 473-88
Authors Levy HR, Christoff M, Ingulli J, Ho EM
Title Glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: revised kinetic mechanism and kinetics of ATP inhibition.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 6655694
Journal J Mol Biol
Year 1983
Volume 171
Pages 233-6
Authors Ammon HL, Murphy KC, Bhattacharjee SK, Szepesi B, Hansen RJ
Title Preliminary crystallographic study of glucose-6-phosphate dehydrogenase from rat liver.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 6696439
Journal Arch Biochem Biophys
Year 1984
Volume 228
Pages 415-24
Authors Viola RE
Title Kinetic studies of the reactions catalyzed by glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: pH variation of kinetic parameters.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 3720867
Journal Exp Eye Res
Year 1986
Volume 42
Pages 489-96
Authors Dovrat A, Scharf J, Eisenbach L, Gershon D
Title G6PD molecules devoid of catalytic activity are present in the nucleus of the rat lens.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 3581436
Journal Cell Biochem Funct
Year 1987
Volume 5
Pages 79-95
Authors Rosemeyer MA
Title The biochemistry of glucose-6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase and glutathione reductase.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 3072957
Journal Biochem Int
Year 1988
Volume 17
Pages 1099-106
Authors Kim YS, Kim YI, Byun HS
Title Inactivation of Saccharomyces cerevisiae glucose-6-phosphate dehydrogenase by diethylpyrocarbonate.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 2590166
Journal Biochem J
Year 1989
Volume 262
Pages 795-800
Authors Aon MA, Cortassa S, Hervagault JF, Thomas D
Title pH-induced bistable dynamic behaviour in the reaction catalysed by glucose-6-phosphate dehydrogenase and conformational hysteresis of the enzyme.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 1304341
Journal Protein Sci
Year 1992
Volume 1
Pages 329-34
Authors Lee WT, Levy HR
Title Lysine-21 of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase participates in substrate binding through charge-charge interaction.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 8495203
Journal Protein Sci
Year 1993
Volume 2
Pages 859-62
Authors Adams MJ, Basak AK, Gover S, Rowland P, Levy HR
Title Site-directed mutagenesis to facilitate X-ray structural studies of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID
PubMed ID 7881907
Journal Structure
Year 1994
Volume 2
Pages 1073-87
Authors Rowland P, Basak AK, Gover S, Levy HR, Adams MJ
Title The three-dimensional structure of glucose 6-phosphate dehydrogenase from Leuconostoc mesenteroides refined at 2.0 A resolution.
Related PDB 1dpg
Related UniProtKB P11411
[12]
Resource
Comments
Medline ID
PubMed ID 7789519
Journal FEBS Lett
Year 1995
Volume 366
Pages 61-4
Authors Bautista JM, Mason PJ, Luzzatto L
Title Human glucose-6-phosphate dehydrogenase. Lysine 205 is dispensable for substrate binding but essential for catalysis.
Related PDB
Related UniProtKB
[13]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT ASN-240, AND MUTAGENESIS OF ASP-177; HIS-178 AND HIS-240.
Medline ID
PubMed ID 9485426
Journal Biochemistry
Year 1998
Volume 37
Pages 2759-67
Authors Cosgrove MS, Naylor C, Paludan S, Adams MJ, Levy HR
Title On the mechanism of the reaction catalyzed by glucose 6-phosphate dehydrogenase.
Related PDB 2dpg
Related UniProtKB P11411
[14]
Resource
Comments
Medline ID
PubMed ID 10089300
Journal Acta Crystallogr D Biol Crystallogr
Year 1999
Volume 55
Pages 826-34
Authors Au SW, Naylor CE, Gover S, Vandeputte-Rutten L, Scopes DA, Mason PJ, Luzzatto L, Lam VM, Adams MJ
Title Solution of the structure of tetrameric human glucose 6-phosphate dehydrogenase by molecular replacement.
Related PDB
Related UniProtKB
[15]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS ASN-177 AND CYS-365 IN COMPLEX WITH NAD; NADP AND SUBSTRATE.
Medline ID
PubMed ID 11106478
Journal Biochemistry
Year 2000
Volume 39
Pages 15002-11
Authors Cosgrove MS, Gover S, Naylor CE, Vandeputte-Rutten L, Adams MJ, Levy HR
Title 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.
Related PDB 1e77 1e7m 1e7y
Related UniProtKB P11411
[16]
Resource
Comments
Medline ID
PubMed ID 11106479
Journal Biochemistry
Year 2000
Volume 39
Pages 15012-21
Authors Vought V, Ciccone T, Davino MH, Fairbairn L, Lin Y, Cosgrove MS, Adams MJ, Levy HR
Title Delineation of the roles of amino acids involved in the catalytic functions of Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 10734064
Journal J Biol Chem
Year 2000
Volume 275
Pages 9256-62
Authors Gomez-Gallego F, Garrido-Pertierra A, Bautista JM
Title Structural defects underlying protein dysfunction in human glucose-6-phosphate dehydrogenase A(-) deficiency.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 10959850
Journal J Org Chem
Year 2000
Volume 65
Pages 4498-508
Authors Berkowitz DB, Bose M, Pfannenstiel TJ, Doukov T
Title alpha-fluorinated phosphonates as substrate mimics for glucose 6-phosphate dehydrogenase: the CHF stereochemistry matters.
Related PDB
Related UniProtKB
[19]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF VARIANT CANTON IN COMPLEX WITH NADP, AND HOMOTETRAMERIZATION.
Medline ID
PubMed ID 10745013
Journal Structure Fold Des
Year 2000
Volume 8
Pages 293-303
Authors Au SW, Gover S, Lam VM, Adams MJ
Title Human glucose-6-phosphate dehydrogenase: the crystal structure reveals a structural NADP(+) molecule and provides insights into enzyme deficiency.
Related PDB 1qki
Related UniProtKB P11413
[20]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11320304
Journal Acta Crystallogr D Biol Crystallogr
Year 2001
Volume 57
Pages 635-48
Authors Naylor CE, Gover S, Basak AK, Cosgrove MS, Levy HR, Adams MJ
Title 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.
Related PDB 1h93 1h94 1h9a 1h9b
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 12033926
Journal Biochemistry
Year 2002
Volume 41
Pages 6939-45
Authors Cosgrove MS, Loh SN, Ha JH, Levy HR
Title The 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.
Related PDB
Related UniProtKB

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.

Created Updated
2004-03-24 2009-02-26