KEGG   ENZYME: 1.1.1.360Help
Entry
EC 1.1.1.360                Enzyme                                 

Name
glucose/galactose 1-dehydrogenase;
GdhA;
dual-specific glucose/galactose dehydrogenase;
glucose (galactose) dehydrogenase;
glucose/galactose dehydrogenase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
D-glucose/D-galactose 1-dehydrogenase (NADPH)
Reaction(IUBMB)
(1) D-glucopyranose + NADP+ = D-glucono-1,5-lactone + NADPH + H+ [RN:R07147];
(2) D-galactopyranose + NADP+ = D-galactono-1,5-lactone + NADPH + H+ [RN:R01096]
Reaction(KEGG)
Substrate
D-glucopyranose [CPD:C00031];
NADP+ [CPD:C00006];
D-galactopyranose [CPD:C00124]
Product
D-glucono-1,5-lactone [CPD:C00198];
NADPH [CPD:C00005];
H+ [CPD:C00080];
D-galactono-1,5-lactone [CPD:C02669]
Comment
A zinc protein. The enzyme from the archaeon Picrophilus torridus is involved in glucose and galactose catabolism via the nonphosphorylative variant of the Entner-Doudoroff pathway. It shows 20-fold higher activity with NADP+ compared to NAD+. The oxidation of D-glucose and D-galactose is catalysed at a comparable rate (cf. EC 1.1.1.119, glucose 1-dehydrogenase (NADP+) and EC 1.1.1.120, galactose 1-dehydrogenase (NADP+)).
History
EC 1.1.1.360 created 2013
Pathway
Pentose phosphate pathway
Galactose metabolism
Biosynthesis of secondary metabolites
Biosynthesis of antibiotics
Orthology
K18124  
glucose/galactose 1-dehydrogenase (NADP+)
Genes
TAC: 
TVO: 
PTO: 
FAC: 
Taxonomy
Reference
1  [PMID:15691337]
  Authors
Angelov A, Futterer O, Valerius O, Braus GH, Liebl W
  Title
Properties of the recombinant glucose/galactose dehydrogenase from the extreme thermoacidophile, Picrophilus torridus.
  Journal
FEBS. J. 272 (2005) 1054-62.
  Sequence
[pto:PTO1070]
Reference
2  [PMID:16556607]
  Authors
Milburn CC, Lamble HJ, Theodossis A, Bull SD, Hough DW, Danson MJ, Taylor GL
  Title
The structural basis of substrate promiscuity in glucose dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus.
  Journal
J. Biol. Chem. 281 (2006) 14796-804.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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