EzCatDB: S00324
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DB codeS00324
RLCP classification9.1050.440000.8010 : Hydride transfer
9.5010.536200.8010 : Hydride transfer
CATH domainDomain 13.40.50.720 : Rossmann foldCatalytic domain
E.C.1.1.1.47

CATH domainRelated DB codes (homologues)
3.40.50.720 : Rossmann foldS00543,S00551,S00552,S00553,S00602,S00604,S00605,S00608,S00610,S00625,S00319,S00328,S00329,S00330,S00331,S00332,D00456,D00457,D00458,S00320,S00325,S00326,S00327,D00459,S00335,S00336,S00334,T00219,S00339,D00513,D00001,D00002,D00003,D00005,D00007,D00008,D00010,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
UniProtKBKEGG

P40288
Protein nameGlucose 1-dehydrogenaseglucose 1-dehydrogenase
D-glucose dehydrogenase (NAD(P)+)
hexose phosphate dehydrogenase
SynonymsEC 1.1.1.47
PfamPF00106 (adh_short)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00030Pentose phosphate pathway

UniProtKB:Accession NumberP40288
Entry nameDHG_BACME
ActivityBeta-D-glucose + NAD(P)(+) = D-glucono-1,5- lactone + NAD(P)H.
SubunitHomotetramer.
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00221C00003C00006C00198C00004C00005C00080
Compoundbeta-D-GlucoseNAD+NADP+D-Glucono-1,5-lactoneNADHNADPHH+
Typecarbohydrateamide group,amine group,nucleotideamide group,amine group,nucleotidecarbohydrateamide group,amine group,nucleotideamide group,amine group,nucleotideothers
ChEBI15903
15846
18009
16217
16908
16474
15378
PubChem64689
5893
5886
7027
439153
5884
1038
               
1g6kAUnboundBound:NADUnboundUnboundUnboundUnbound 
1g6kBUnboundBound:NADUnboundUnboundUnboundUnbound 
1g6kEUnboundBound:NADUnboundUnboundUnboundUnbound 
1g6kFUnboundBound:NADUnboundUnboundUnboundUnbound 
1gcoAUnboundBound:NADUnboundUnboundUnboundUnbound 
1gcoBUnboundBound:NADUnboundUnboundUnboundUnbound 
1gcoEUnboundBound:NADUnboundUnboundUnboundUnbound 
1gcoFUnboundBound:NADUnboundUnboundUnboundUnbound 
1geeAUnboundBound:NADUnboundUnboundUnboundUnbound 
1geeBUnboundBound:NADUnboundUnboundUnboundUnbound 
1geeEUnboundBound:NADUnboundUnboundUnboundUnbound 
1geeFUnboundBound:NADUnboundUnboundUnboundUnbound 
1rwbAUnboundBound:NADUnboundUnboundUnboundUnbound 
1rwbBUnboundBound:NADUnboundUnboundUnboundUnbound 
1rwbEUnboundBound:NADUnboundUnboundUnboundUnbound 
1rwbFUnboundBound:NADUnboundUnboundUnboundUnbound 

Active-site residues
resource
Swiss-prot;P40288
pdbCatalytic residuescomment
          
1g6kASER 145;TYR 158;LYS 162
mutant E96A
1g6kBSER 145;TYR 158;LYS 162
mutant E96A
1g6kESER 145;TYR 158;LYS 162
mutant E96A
1g6kFSER 145;TYR 158;LYS 162
mutant E96A
1gcoASER 145;TYR 158;LYS 162
 
1gcoBSER 145;TYR 158;LYS 162
 
1gcoESER 145;TYR 158;LYS 162
 
1gcoFSER 145;TYR 158;LYS 162
 
1geeASER 145;TYR 158;LYS 162
mutant Q252L
1geeBSER 145;TYR 158;LYS 162
mutant Q252L
1geeESER 145;TYR 158;LYS 162
mutant Q252L
1geeFSER 145;TYR 158;LYS 162
mutant Q252L
1rwbASER 145;TYR 158;LYS 162
mutant E170K, Q252L
1rwbBSER 145;TYR 158;LYS 162
mutant E170K, Q252L
1rwbESER 145;TYR 158;LYS 162
mutant E170K, Q252L
1rwbFSER 145;TYR 158;LYS 162
mutant E170K, Q252L

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]p.308

references
[1]
PubMed ID3113945
JournalEur J Biochem
Year1987
Volume167
Pages123-4
AuthorsPal GP, Jany KD, Saenger W
TitleCrystallization of and X-ray investigations on glucose dehydrogenase from Bacillus megaterium.
[2]
PubMed ID2803257
JournalBiochem J
Year1989
Volume261
Pages973-7
AuthorsSmith LD, Budgen N, Bungard SJ, Danson MJ, Hough DW
TitlePurification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum.
[3]
PubMed ID2503396
JournalFEBS Lett
Year1989
Volume253
Pages113-6
AuthorsNagao T, Makino Y, Yamamoto K, Urabe I, Okada H
TitleStability-increasing mutants of glucose dehydrogenase.
[4]
PubMed ID2495285
JournalJ Biol Chem
Year1989
Volume264
Pages6381-5
AuthorsMakino Y, Negoro S, Urabe I, Okada H
TitleStability-increasing mutants of glucose dehydrogenase from Bacillus megaterium IWG3.
[5]
PubMed ID1915348
JournalEur J Biochem
Year1991
Volume200
Pages759-66
AuthorsYomo T, Urabe I, Okada H
TitlePreparation and kinetic properties of 5-ethylphenazine-glucose-dehydrogenase-NAD+ conjugate, a semisynthetic glucose oxidase.
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH NAD.
PubMed ID11173533
JournalJ Biochem (Tokyo)
Year2001
Volume129
Pages303-12
AuthorsYamamoto K, Kurisu G, Kusunoki M, Tabata S, Urabe I, Osaki S
TitleCrystal structure of glucose dehydrogenase from Bacillus megaterium IWG3 at 1.7 A resolution.
Related PDB1gco
Related UniProtKBP40288
[7]
PubMed ID12743762
JournalAppl Microbiol Biotechnol
Year2003
Volume61
Pages329-35
AuthorsBaik SH, Ide T, Yoshida H, Kagami O, Harayama S
TitleSignificantly enhanced stability of glucose dehydrogenase by directed evolution.
[8]
PubMed ID15933031
JournalAppl Environ Microbiol
Year2005
Volume71
Pages3285-93
AuthorsBaik SH, Michel F, Aghajari N, Haser R, Harayama S
TitleCooperative effect of two surface amino acid mutations (Q252L and E170K) in glucose dehydrogenase from Bacillus megaterium IWG3 on stabilization of its oligomeric state.
Related PDB1rwb

comments
There are several types of glucose dehydrogenase such as PQQ-dependent GDH (E.C. 1.1.5.2), "short" NAD(P)-dependent GDH (E.C. 1.1.1.47), "long" NAD(P)-dependent GDH.
This enzyme belongs to "short" NAD(P)-dependent GDH (E.C. 1.1.1.47).
This enzyme has got the same catalytic triad (Ser/Tyr/Lys) as those of Drosophia alcohol dehydrogenase (E.C. 1.1.1.1; S00319 in EzCatDB) and tetrahydroxynaphthalene reductase (E.C. 1.1.1.252; S00336 in EzCatDB). Thus, it must have a similar catalytic reaction mechanism to those enzymes.

createdupdated
2005-01-202011-06-23


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