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Article

C2α-carbanion-protonating glutamate discloses tradeoffs between substrate accommodation and reaction rate in actinobacterial 2-hydroxyacyl-CoA lyase.

FEBS open bio - 1 Jul 2026

Zahn Michael, Seroka Barbara, Lazny Ryszard, Lotowski Zenon, Rohwerder Thore

Abstract excerpt

Thiamine-dependent actinobacterial 2-hydroxyacyl-CoA lyase (AcHACL) catalyzes the reversible cleavage of 2-hydroxyacyl-CoAs to formyl-CoA and carbonyl compounds. To exploit the enzyme's biotechnological potential, a deeper understanding of the catalysis is required. Previously, AcHACL E493 was identified as an important acid/base catalyst. Here, wild-type and E493 mutant crystal structures representing Michaelis...

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PMID: 41606311
DOI: 10.1002/2211-5463.70199
PMCID: PMC13327070

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