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Interacting selectively and non-covalently with nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP, or the reduced form, NADPH. Interacting selectively and non-covalently with a coenzyme, any of various nonprotein organic cofactors that are required, in addition to an enzyme and a substrate, for an enzymatic reaction to proceed. Interacting selectively and non-covalently with a cofactor, a substance that is required for the activity of an enzyme or other protein. Cofactors may be inorganic, such as the metal atoms zinc, iron, and copper in certain forms, or organic, in which case they are referred to as coenzymes. Cofactors may either be bound tightly to active sites or bind loosely with the substrate. Interacting selectively and non-covalently with lipoic acid, 1,2-dithiolane-3-pentanoic acid. Interacting selectively and non-covalently with FMN, flavin mononucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. Interacting selectively and non-covalently with FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. Interacting selectively and non-covalently with thiamin pyrophosphate, the diphosphoric ester of thiamin. Acts as a coenzyme of several (de)carboxylases, transketolases, and alpha-oxoacid dehydrogenases. Interacting selectively and non-covalently with F420, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. Interacting selectively and non-covalently with the molybdopterin cofactor (Moco), essential for the catalytic activity of some enzymes, e.g. sulfite oxidase, xanthine dehydrogenase, and aldehyde oxidase. The cofactor consists of a mononuclear molybdenum (Mo-molybdopterin) or tungsten ion (W-molybdopterin) coordinated by one or two molybdopterin ligands. Interacting selectively and non-covalently with nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD, or the reduced form, NADH. The selective, non-covalent, often stoichiometric, interaction of a molecule with one or more specific sites on another molecule. Interacting selectively and non-covalently with a tetrahydrobiopterin, 5,6,7,8-tetrahydrobiopterin or a derivative thereof; tetrahydrobiopterins are enzyme cofactors that carry electrons in redox reactions. Interacting selectively and non-covalently with acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with a fatty acyl group.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: coenzyme binding
Acc: GO:0050662
Aspect: Molecular Function
Desc: Interacting selectively and non-covalently with a coenzyme, any of various nonprotein organic cofactors that are required, in addition to an enzyme and a substrate, for an enzymatic reaction to proceed.
Proteins in PDR annotated with:
   This term: 194 [Search]
   Term or descendants: 1482 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0050662 - coenzyme binding (interactive image map)
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