Enzyme

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     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.1 With NAD+ or NADP+ as acceptor
ID:1.1.1.360
Description:Glucose/galactose 1-dehydrogenase.
Alternative Name: Glucose/galactose dehydrogenase.
Glucose (galactose) dehydrogenase.
Dual-specific glucose/galactose dehydrogenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.1.360
BRENDA Enzyme Link: BRENDA 1.1.1.360
KEGG Enzyme Link: KEGG1.1.1.360
BioCyc Enzyme Link: BioCyc 1.1.1.360
ExPASy Enzyme Link: ExPASy1.1.1.360
EC2PDB Enzyme Link: EC2PDB 1.1.1.360
ExplorEnz Enzyme Link: ExplorEnz 1.1.1.360
PRIAM enzyme-specific profiles Link: PRIAM 1.1.1.360
IntEnz Enzyme Link: IntEnz 1.1.1.360
MEDLINE Enzyme Link: MEDLINE 1.1.1.360
MSA:

1.1.1.360;

Phylogenetic Tree:

1.1.1.360;

Uniprot:
M-CSA:
RHEA:18625 D-galactose + NADP(+) = D-galactono-1,5-lactone + H(+) + NADPH
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1
Reaction
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References

TitleAuthorsDatePubMed ID
Some physical properties of three sugar dehydrogenases from a pseudomonad.Cline AL, Hu AS1965 Nov5845849
Enzymatic characterization and comparison of three sugar dehydrogenases from a pseudomonad.Cline AL, Hu AS1965 Nov5845848
The isolation of three sugar dehydrogenases from a psuedomonad.Cline AL, Hu AS1965 Nov5845847
[Degradation of deoxysurgars by bacterial enzymes. V. Purification and characterization of an NADP-dependent abequose dehydrogenase from Pseudomonas putida].Schiwara HW, Domagk GF1968 Oct4387016

RHEA:14405 D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[n+;H0:6]1:[cH;+0:7]:[cH;+0:8]:[cH;+0:9]:[c;H0;+0:10](-[*:11]):[cH;+0:12]:1>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].[*:5]-[N;H0;+0:6]1-[CH;+0:7]=[CH;+0:8]-[CH2;+0:9]-[C;H0;+0:10](-[*:11])=[CH;+0:12]-1
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Carbohydrate metabolism in Thermoproteus tenax: in vivo utilization of the non-phosphorylative Entner-Doudoroff pathway and characterization of its first enzyme, glucose dehydrogenase.Siebers B, Wendisch VF, Hensel R1997 Aug9238103
Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: enzyme purification, characterisation and N-terminal sequence.Bonete MJ, Pire C, LLorca FI, Camacho ML1996 Apr 18925901
Cloning, sequencing and expression of the gene encoding glucose dehydrogenase from the thermophilic archaeon Thermoplasma acidophilum.Bright JR, Byrom D, Danson MJ, Hough DW, Towner P1993 Feb 18436115
Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus.Giardina P, de Biasi MG, de Rosa M, Gambacorta A, Buonocore V1986 Nov 13827812
Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum.Smith LD, Budgen N, Bungard SJ, Danson MJ, Hough DW1989 Aug 12803257
The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.Milburn CC, Lamble HJ, Theodossis A, Bull SD, Hough DW, Danson MJ, Taylor GL2006 May 2616556607
Properties of the recombinant glucose/galactose dehydrogenase from the extreme thermoacidophile, Picrophilus torridus.Angelov A, Fütterer O, Valerius O, Braus GH, Liebl W2005 Feb15691337
Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase.Lamble HJ, Heyer NI, Bull SD, Hough DW, Danson MJ2003 Sep 512824170
Heterologous overexpression of glucose dehydrogenase from the halophilic archaeon Haloferax mediterranei, an enzyme of the medium chain dehydrogenase/reductase family.Pire C, Esclapez J, Ferrer J, Bonete MJ2001 Jun 2511425479