09-15-2021-0333 - Amine Oxidase Oxidoreducase

 An amine oxidase is an enzyme that catalyzes the oxidative cleavage of alkylamines into aldehydes and ammonia:^[1]

RCH₂NH₂ + H₂O + O₂  RCHO + NH₃ + H₂O₂

Amine oxidases are divided into two subfamilies based on the cofactor they contain:

Class	Cofactor	Subclass	Enzyme Commission number	Human genes
Amine oxidase (formerly EC 1.4.3.6)	copper	lysyl oxidase	EC 1.4.3.13	LOX
		primary-amine oxidase	EC 1.4.3.21	AOC2, AOC3
		diamine oxidase	EC 1.4.3.22	AOC1
Monoamine oxidase	flavin	N/A	EC 1.4.3.4	MAOA, MAOB

References[edit]

1. ^ Mondovì B, Finazzi Agrò A (1982). "Structure and function of amine oxidase". Advances in Experimental Medicine and Biology. Advances in Experimental Medicine and Bioligy. 148: 141–53. doi:10.1007/978-1-4615-9281-5_12. ISBN 978-1-4615-9283-9. PMID 7124512.

https://en.wikipedia.org/wiki/Amine_oxidase


In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors.[1][2] Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix.[3]
https://en.wikipedia.org/wiki/Oxidoreductase

Metalloprotein is a generic term for a protein that contains a metal ion cofactor.^[1][2] A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins (out of ~20,000) contain zinc-binding protein domains^[3] although there may be up to 3000 human zinc metalloproteins.^[4]

The structure of hemoglobin. The heme cofactor, containing the metal iron, shown in green.

https://en.wikipedia.org/wiki/Metalloprotein