Cysteine S-conjugate sulfoxide β-lyase activity for human ACCS.

Jinmin Gao, Yueqi Xu, Christopher Yeh, Yike Zou, Yang Hai

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Article in The FEBS journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

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5 authors.

Jinmin GaoDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.

Yueqi XuDepartment of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA, USA.

Christopher YehDepartment of Molecular, Cellular, and Developmental Biology, University of California, Santa Barbara, CA, USA.

Yike ZouSchool of Pharmaceutical Sciences, Shanghai Jiao Tong University, China.

Yang HaiDepartment of Chemistry and Biochemistry, University of California, Santa Barbara, CA, USA.ORCID 0000-0002-2039-5367

Funding

Understanding the specificity and non-native catalytic activity of PLP-dependent enzymesR35GM151205 · NIGMS · UNIVERSITY OF CALIFORNIA SANTA BARBARA · PI Yang Hai · 2023 to 2026

$1.8M

NIGMS NIH HHS R35 GM151205NIGMS NIH HHS R35GM151205

6 · The paper itself

Abstract

1-Aminocyclopropane-1-carboxylate synthase (ACCS) catalyzes the conversion of S-adenosyl-methionine to 1-aminocyclopropane-1-carboxylate (ACC), a rate-limiting step in ethylene biosynthesis. A gene encoding a putative ACCS protein was identified in the human genome two decades ago. It has been shown to not exhibit any canonical ACC synthase activity and its true function remains obscure. In this study, through a biochemical profiling approach, we demonstrate that human ACCS possesses cysteine conjugate sulfoxide β-lyase activity. This function is unexpected but reasonable, as it somewhat parallels the activity of ACCS proteins found in non-seed plants. Structure-function relationship study of human ACCS, guided by an AlphaFold2 model, allowed us to identify key active site residues that are important for its β-lyase activity. Our biochemical study of human ACCS also provided insights into the function of other mammalian ACCS homologs.

Indexed as

Carbon-Sulfur LyasesCysteineLyasesAmino Acid SequenceCatalytic DomainHumansModels, MolecularStructure-Activity Relationship1-aminocyclopropanecarboxylate synthaseCarbon-Sulfur LyasesCysteineLyasescatalysisenzymePLPpseudoenzymePUF

Identifiers

PMID39876065

DOI10.1111/febs.17419

PMCPMC12064363

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.