Choline oxidase

Class of enzymes From Wikipedia, the free encyclopedia

In enzymology, choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes two consecutive chemical reactions

2D representation of the chemical structure of choline .
choline
 
O2
H2O2
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
O2
H2O2
 
2D representation of the chemical structure of glycine betaine aldehyde .
glycine betaine aldehyde
2D representation of the chemical structure of glycine betaine aldehyde .
glycine betaine aldehyde
 
O2
H2O2
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
O2
H2O2
 
2D representation of the chemical structure of trimethylglycine .
trimethylglycine
EC no.1.1.3.17
CAS no.9028-67-5
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Choline oxidase
Choline oxidase dimer, Arthrobacter globiformis
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EC no.1.1.3.17
CAS no.9028-67-5
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The two substrates of this enzyme are choline and oxygen. The first reaction gives betaine aldehyde and hydrogen peroxide. The aldehyde intermediate is then further oxidised to trimethylglycine.[1][2]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is choline:oxygen 1-oxidoreductase. This enzyme participates in glycine, serine, and threonine metabolism. It employs one cofactor, FAD.[3][4][5][6]

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