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Enzymes regulated via cystathionine β-synthase domains

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Abstract

Cystathionine β-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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Abbreviations

AdoMet:

S-adenosyl-L-methionine

AID:

auto-inhibitory domain

AMPK:

AMP-activated protein kinase

CBS:

cystathionine β-synthase

dCBS:

Drosophila melanogaster CBS

hCBS:

human CBS

yCBS:

yeast Saccharomyces cerevisiae CBS

IMPDH:

inosine-5′-monophosphate dehydroge-nase

MTA:

5′-methylthioadenosine

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Authors and Affiliations

  1. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119992, Moscow, Russia

    V. A. Anashkin & A. A. Baykov

  2. Department of Biochemistry, University of Turku, FIN-20014, Turku, Finland

    R. Lahti

Authors
  1. V. A. Anashkin
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  2. A. A. Baykov
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  3. R. Lahti
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Correspondence to A. A. Baykov.

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Original Russian Text © V. A. Anashkin, A. A. Baykov, R. Lahti, 2017, published in Biokhimiya, 2017, Vol. 82, No. 10, pp. 1417-1426.

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Anashkin, V.A., Baykov, A.A. & Lahti, R. Enzymes regulated via cystathionine β-synthase domains. Biochemistry Moscow 82, 1079–1087 (2017). https://doi.org/10.1134/S0006297917100017

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