Literature summary for 1.14.13.225 extracted from

McDonald, C.A.; Liu, Y.Y.; Palfey, B.A.
Actin stimulates reduction of the MICAL-2 monooxygenase domain (2013), Biochemistry, 52, 6076-6084.

Search for more literature for 1.14.13.225

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q8BML1	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the reductive half-reaction of the mical2 hydroxylase domain is stimulated by F-actin. In the absence of actin, NADPH reduces the flavin relatively slowly. Actin speeds that reaction significantly. The separate monooxygenase domain has the classic regulatory behavior of flavin-dependent aromatic hydroxylases (Class A monooxygenases) with slow reduction of the flavin when the substrate to be oxygenated is absent	Mus musculus	?	-	?
[F-actin]-L-methionine + NADPH + O2 + H+	-	Mus musculus	[F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O	-	?

Synonyms

Synonyms	Comment	Organism
MICAL-2	-	Mus musculus
Mical2	-	Mus musculus

Cofactor

Cofactor	Comment	Organism	Structure
NADH	strong preference for NADPH over NADH caused by a large difference in binding	Mus musculus
NADPH	strong preference for NADPH over NADH caused by a large difference in binding. Mical22 is specific for the proR hydride of NADPH, with a 4.8fold kinetic isotope effect	Mus musculus

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Release 2023.1 (January 2023)