KEGG   ENZYME: 1.1.3.8Help
Entry
EC 1.1.3.8                  Enzyme                                 

Name
L-gulonolactone oxidase;
L-gulono-gamma-lactone: O2 oxidoreductase;
L-gulono-gamma-lactone oxidase;
L-gulono-gamma-lactone:oxidoreductase;
GLO
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
L-gulono-1,4-lactone:oxygen 3-oxidoreductase
Reaction(IUBMB)
L-gulono-1,4-lactone + O2 = L-ascorbate + H2O2 (overall reaction) [RN:R10053];
(1a) L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2 [RN:R03184];
(1b) L-xylo-hex-2-ulono-1,4-lactone = L-ascorbate (spontaneous) [RN:R00647]
Reaction(KEGG)
Substrate
L-gulono-1,4-lactone [CPD:C01040];
O2 [CPD:C00007];
L-xylo-hex-2-ulono-1,4-lactone [CPD:C03289]
Product
L-ascorbate [CPD:C00072];
H2O2 [CPD:C00027];
L-xylo-hex-2-ulono-1,4-lactone [CPD:C03289]
Comment
A microsomal flavoprotein (FAD). The product spontaneously isomerizes to L-ascorbate. While most higher animals can synthesize asborbic acid, primates and guinea pigs cannot [3].
History
EC 1.1.3.8 created 1965, modified 2001, modified 2006
Pathway
Ascorbate and aldarate metabolism
Metabolic pathways
Orthology
K00103  
L-gulonolactone oxidase
Genes
MMU: 
268756(Gulo)
RNO: 
60671(Gulo)
CGE: 
100760306(Gulo)
HGL: 
TUP: 
CFA: 
AML: 
FCA: 
PTG: 
BTA: 
286812(GULO)
BOM: 
PHD: 
CHX: 
SSC: 
396759(GULO)
CFR: 
BACU: 
LVE: 
ECB: 
PALE: 
MDO: 
SHR: 
OAA: 
GGA: 
MGP: 
FAB: 
PHI: 
APLA: 
FPG: 
FCH: 
CLV: 
ASN: 
AMJ: 
PSS: 
ACS: 
XLA: 
XTR: 
LCM: 
BFO: 
CIN: 
SPU: 
ISC: 
NVE: 
TAD: 
AQU: 
GSL: 
LBC: 
ACAN: 
LMA: 
LIF: 
LBZ: 
NGR: 
LPN: 
LPM: 
LPF: 
LPP: 
LPC: 
LPA: 
BUR: 
BME: 
BMF: 
GBE: 
OIH: 
MTU: 
MTC: 
MRA: 
MTF: 
MTB: 
MBO: 
MBT: 
MUL: 
MMI: 
NFA: 
RHA: 
RER: 
ROP: 
SCO: 
SCO5857(SC9B10.24c)
FRA: 
SEN: 
SVI: 
STP: 
SAQ: 
MAU: 
MIL: 
CWO: 
NPU: 
 » show all
Taxonomy
Reference
1  [PMID:14405898]
  Authors
ISHERWOOD FA, MAPSON LW, CHEN YT.
  Title
Synthesis of L-ascorbic acid in rat-liver homogenates. Conversion of L-gulono- and L-galactono-gamma-lactone and the respective acids into L-ascorbic acid.
  Journal
Biochem. J. 76 (1960) 157-71.
  Organism
Rattus norvegicus
Reference
2  [PMID:7138847]
  Authors
Kiuchi K, Nishikimi M, Yagi K.
  Title
Purification and characterization of L-gulonolactone oxidase from chicken kidney microsomes.
  Journal
Biochemistry. 21 (1982) 5076-82.
  Organism
Gallus gallus
Reference
3  [PMID:8175804]
  Authors
Nishikimi M, Fukuyama R, Minoshima S, Shimizu N, Yagi K.
  Title
Cloning and chromosomal mapping of the human nonfunctional gene for L-gulono-gamma-lactone oxidase, the enzyme for L-ascorbic acid biosynthesis missing in man.
  Journal
J. Biol. Chem. 269 (1994) 13685-8.
Reference
4
  Authors
Chatterjee, I.B., Chatterjee, G.C., Ghosh, N.C. and Guha, B.C.
  Title
Identification of 2-keto-L-gulonolactone as an intermediate in the biosynthesis of L-ascorbic acid.
  Journal
Naturwissenschaften 46 (1959) 475.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9028-78-8

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