A2 Refereed review article in a scientific journal
Enzymes regulated via cystathionine beta-synthase domains
Authors: Anashkin VA, Baykov AA, Lahti R
Publisher: MAIK NAUKA/INTERPERIODICA/SPRINGER
Publishing place: Moscow
Publication year: 2017
Journal: Биохимия / Biochemistry
Journal name in source: BIOCHEMISTRY-MOSCOW
Journal acronym: BIOCHEMISTRY-MOSCOW+
Volume: 82
Issue: 10
First page : 1079
Last page: 1087
Number of pages: 9
ISSN: 0006-2979
eISSN: 1608-3040
DOI: https://doi.org/10.1134/S0006297917100017
Abstract
Cystathionine beta-synthase (CBS) domains discovered 20 years ago can bind different adenosine derivatives (AMP, ADP, ATP, S-adenosylmethionine, NAD, diadenosine polyphosphates) and thus regulate the activities of numerous proteins. Mutations in CBS domains of enzymes and membrane transporters are associated with several hereditary diseases. The regulatory unit is a quartet of CBS domains that belong to one or two polypeptides and usually form a conserved disk-like structure. CBS domains function as "internal inhibitors" in enzymes, and their bound ligands either amplify or attenuate the inhibitory effect. Recent studies have opened a way to understanding the structural basis of enzyme regulation via CBS domains and widened the list of their bound ligands.
Cystathionine beta-synthase (CBS) domains discovered 20 years ago can bind different adenosine derivatives (AMP, ADP, ATP, S-adenosylmethionine, NAD, diadenosine polyphosphates) and thus regulate the activities of numerous proteins. Mutations in CBS domains of enzymes and membrane transporters are associated with several hereditary diseases. The regulatory unit is a quartet of CBS domains that belong to one or two polypeptides and usually form a conserved disk-like structure. CBS domains function as "internal inhibitors" in enzymes, and their bound ligands either amplify or attenuate the inhibitory effect. Recent studies have opened a way to understanding the structural basis of enzyme regulation via CBS domains and widened the list of their bound ligands.
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