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EC 1.3.3.16 Details
show Brenda entryEC number
1.3.3.16
Accepted name
oxazoline dehydrogenase
Reaction
(1) a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline + O2 = a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole + H2O2;;(2) a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline + O2 = a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole + H2O2;;(3) a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-2-oxazoline + O2 = a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-5-methyl-1,3-oxazole + H2O2
Other name(s)
azoline oxidase,
thiazoline oxidase,
cyanobactin oxidase,
patG (gene name),
mcaG (gene name),
artG (gene name),
lynG (gene name),
tenG (gene name)
Systematic name
a [protein]-2-oxazoline:oxygen oxidoreductase (2-oxazole-forming)
Comment
Contains FMN. This enzyme oxidizes 2-oxazoline, 5-methyl-2-oxazoline, and 2-thiazoline within peptides, which were formed by EC 6.2.2.2, oxazoline synthase, and EC 6.2.2.3, thiazoline synthase, to the respective pyrrole-type rings. The enzyme is found as either a stand-alone protein or as a domain within a multifunctional protein (the G protein) that also functions as a peptidase.
History
created 2020
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1 Oxidoreductases
1.1.1 With NAD+ or NADP+ as acceptor
1.1.3.1 created 1961, deleted 1984 1.1.3.25 created 1986, deleted 2005 1.1.3.26 created 1989, deleted 2002 1.1.3.31 created 1992, deleted 2003 1.1.3.32 created 1999, deleted 2002 1.1.3.33 created 1999, deleted 2002 1.1.3.34 created 1999, deleted 2002 1.1.3.35 created 1999, deleted 2002 1.1.3.36 created 1999, deleted 2002 1.1.99.15 created 1978, deleted 1980 1.1.99.17 created 1982, deleted 2003 1.3.3.2 created 1972, deleted 2005
