KEGG   ENZYME: 1.1.1.359Help
Entry
EC 1.1.1.359                Enzyme                                 

Name
aldose 1-dehydrogenase [NAD(P)+]
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
an aldopyranose:NAD(P)+ 1-oxidoreductase
Reaction(IUBMB)
an aldopyranose + NAD(P)+ = an aldono-1,5-lactone + NAD(P)H + H+ [RN:R10428 R10429]
Reaction(KEGG)
Substrate
aldopyranose [CPD:C20655];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]
Product
aldono-1,5-lactone [CPD:C20616];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
The enzyme from the archaeon Sulfolobus solfataricus shows broad specificity towards aldoses (D-glucose, D-galactose, D-xylose, L-arabinose, 6-deoxy-D-glucose, D-fucose) and can utilize NAD+ and NADP+ with similar catalytic efficiency. It is involved in aldose catabolism via the branched variant of the Entner-Doudoroff pathway.
History
EC 1.1.1.359 created 2013
Pathway
Pentose phosphate pathway
Galactose metabolism
Metabolic pathways
Biosynthesis of secondary metabolites
Biosynthesis of antibiotics
Orthology
K18125  
aldose 1-dehydrogenase [NAD(P)+]
Genes
PTO: 
FAC: 
FAI: 
CDIV: 
SSO: 
SSO3003(dhg-1) SSO3042(dhg-2) SSO3204(dhg-3)
SOL: 
SSOA: 
SSOL: 
SSOF: 
STO: 
SAI: 
Saci_1079
SACN: 
SacN8_05250
SACR: 
SacRon12I_05240
SACS: 
SUSAZ_05025
SIS: 
LS215_2319 LS215_2487 LS215_2525
SIA: 
M1425_2156 M1425_2315 M1425_2353
SIM: 
M1627_2236 M1627_2394 M1627_2431
SID: 
M164_2160 M164_2317 M164_2360
SIY: 
YG5714_2283 YG5714_2452 YG5714_2497
SIN: 
YN1551_0407 YN1551_0458 YN1551_0633
SII: 
LD85_2423 LD85_2603 LD85_2656
SIH: 
SiH_2102 SiH_2256 SiH_2295
SIR: 
SiRe_2034 SiRe_2200 SiRe_2243
SIC: 
SiL_2009 SiL_2165 SiL_2203
SULA: 
BFU36_06060 BFU36_07060 BFU36_07270
MSE: 
Msed_1301
MCN: 
Mcup_0902
AHO: 
Ahos_2067
AMAN: 
B6F84_01630 B6F84_05020
CMA: 
Cmaq_1714
 » show all
Taxonomy
Reference
1  [PMID:3827812]
  Authors
Giardina P, de Biasi MG, de Rosa M, Gambacorta A, Buonocore V
  Title
Glucose dehydrogenase from the thermoacidophilic archaebacterium Sulfolobus solfataricus.
  Journal
Biochem. J. 239 (1986) 517-22.
Reference
2  [PMID:2803257]
  Authors
Smith LD, Budgen N, Bungard SJ, Danson MJ, Hough DW
  Title
Purification and characterization of glucose dehydrogenase from the thermoacidophilic archaebacterium Thermoplasma acidophilum.
  Journal
Biochem. J. 261 (1989) 973-7.
Reference
3  [PMID:12824170]
  Authors
Lamble HJ, Heyer NI, Bull SD, Hough DW, Danson MJ
  Title
Metabolic pathway promiscuity in the archaeon Sulfolobus solfataricus revealed by studies on glucose dehydrogenase and 2-keto-3-deoxygluconate aldolase.
  Journal
J. Biol. Chem. 278 (2003) 34066-72.
  Sequence
[sso:SSO3003]
Reference
4  [PMID:16508107]
  Authors
Theodossis A, Milburn CC, Heyer NI, Lamble HJ, Hough DW, Danson MJ, Taylor GL
  Title
Preliminary crystallographic studies of glucose dehydrogenase from the promiscuous Entner-Doudoroff pathway in the hyperthermophilic archaeon Sulfolobus solfataricus.
  Journal
Acta. Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 61 (2005) 112-5.
Reference
5  [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.
  Sequence
[sso:SSO3003]
Reference
6  [PMID:21265750]
  Authors
Haferkamp P, Kutschki S, Treichel J, Hemeda H, Sewczyk K, Hoffmann D, Zaparty M, Siebers B
  Title
An additional glucose dehydrogenase from Sulfolobus solfataricus: fine-tuning of  sugar degradation?
  Journal
Biochem. Soc. Trans. 39 (2011) 77-81.
  Sequence
[sso:SSO3003]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
DBGET integrated database retrieval system