KEGG   ENZYME: 1.1.3.17Help
Entry
EC 1.1.3.17                 Enzyme                                 

Name
choline oxidase
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With oxygen as acceptor
BRITE hierarchy
Sysname
choline:oxygen 1-oxidoreductase
Reaction(IUBMB)
choline + 2 O2 + H2O = betaine + 2 H2O2 (overall reaction) [RN:R08212];
(1a) choline + O2 = betaine aldehyde + H2O2 [RN:R01022];
(1b) betaine aldehyde + O2 + H2O = betaine + H2O2 [RN:R08211]
Reaction(KEGG)
Substrate
choline [CPD:C00114];
O2 [CPD:C00007];
H2O [CPD:C00001];
betaine aldehyde [CPD:C00576]
Product
betaine [CPD:C00719];
H2O2 [CPD:C00027];
betaine aldehyde [CPD:C00576]
Comment
A flavoprotein (FAD). In many bacteria, plants and animals, the osmoprotectant betaine is synthesized using different enzymes to catalyse the conversion of (1) choline into betaine aldehyde and (2) betaine aldehyde into betaine. In plants, the first reaction is catalysed by EC 1.14.15.7, choline monooxygenase, whereas in animals and many bacteria, it is catalysed by either membrane-bound choline dehydrogenase (EC 1.1.99.1) or soluble choline oxidase (EC 1.1.3.17) [6]. The enzyme involved in the second step, EC 1.2.1.8, betaine-aldehyde dehydrogenase, appears to be the same in those plants, animals and bacteria that use two separate enzymes.
Pathway
Glycine, serine and threonine metabolism
Orthology
K17755  
choline oxidase
Genes
ART: 
AAU: 
ACH: 
AAI: 
ARR: 
Taxonomy
Reference
1  [PMID:599154]
  Authors
Ikuta S, Imamura S, Misaki H, Horiuti Y.
  Title
Purification and characterization of choline oxidase from Arthrobacter globiformis.
  Journal
J. Biochem. (Tokyo). 82 (1977) 1741-9.
  Organism
Arthrobacter globiformis
Reference
2  [PMID:1987142]
  Authors
Rozwadowski KL, Khachatourians GG, Selvaraj G.
  Title
Choline oxidase, a catabolic enzyme in Arthrobacter pascens, facilitates adaptation to osmotic stress in Escherichia coli.
  Journal
J. Bacteriol. 173 (1991) 472-8.
  Organism
Arthrobacter pascens
Reference
3  [PMID:12795615]
  Authors
Rand T, Halkier T, Hansen OC.
  Title
Structural characterization and mapping of the covalently linked FAD cofactor in choline oxidase from Arthrobacter globiformis.
  Journal
Biochemistry. 42 (2003) 7188-94.
  Organism
Arthrobacter globiformis
  Sequence
[arr:ARUE_c04830] (Arthrobacter sp.)
Reference
4  [PMID:15369826]
  Authors
Gadda G, Powell NL, Menon P.
  Title
The trimethylammonium headgroup of choline is a major determinant for substrate binding and specificity in choline oxidase.
  Journal
Arch. Biochem. Biophys. 430 (2004) 264-73.
  Organism
Arthrobacter globiformis
Reference
5  [PMID:15713082]
  Authors
Fan F, Gadda G.
  Title
On the catalytic mechanism of choline oxidase.
  Journal
J. Am. Chem. Soc. 127 (2005) 2067-74.
  Organism
Arthrobacter globiformis
Reference
6  [PMID:12466265]
  Authors
Waditee R, Tanaka Y, Aoki K, Hibino T, Jikuya H, Takano J, Takabe T, Takabe T.
  Title
Isolation and functional characterization of N-methyltransferases that catalyze betaine synthesis from glycine in a halotolerant photosynthetic organism Aphanothece halophytica.
  Journal
J. Biol. Chem. 278 (2003) 4932-42.
  Organism
Aphanothece halophytica
Reference
7  [PMID:14678796]
  Authors
Fan F, Ghanem M, Gadda G.
  Title
Cloning, sequence analysis, and purification of choline oxidase from Arthrobacter globiformis: a bacterial enzyme involved in osmotic stress tolerance.
  Journal
Arch. Biochem. Biophys. 421 (2004) 149-58.
  Organism
Arthrobacter globiformis
  Sequence
[arr:ARUE_c04830] (Arthrobacter sp.)
Reference
8  [PMID:12637017]
  Authors
Gadda G.
  Title
Kinetic mechanism of choline oxidase from Arthrobacter globiformis.
  Journal
Biochim. Biophys. Acta. 1646 (2003) 112-8.
  Organism
Arthrobacter globiformis
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9028-67-5

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