Enzymes regulated via cystathionine beta-synthase domains



: Anashkin VA, Baykov AA, Lahti R

Publisher: MAIK NAUKA/INTERPERIODICA/SPRINGER

: Moscow

: 2017

: Биохимия / Biochemistry

: BIOCHEMISTRY-MOSCOW

: BIOCHEMISTRY-MOSCOW+

: 82

: 10

: 1079

: 1087

: 9

: 0006-2979

: 1608-3040

DOI: https://doi.org/10.1134/S0006297917100017


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.



Last updated on 2024-26-11 at 21:17