Clostridial glycine reductase: protein C, the acetyl group acceptor, catalyzes the arsenate-dependent decomposition of acetyl phosphate. | Zendy

Thressa C. Stadtman | Zendy

Open Access

Clostridial glycine reductase: protein C, the acetyl group acceptor, catalyzes the arsenate-dependent decomposition of acetyl phosphate.

Author(s) -

Thressa C. Stadtman

Publication year - 1989

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.86.20.7853

Subject(s) - arsenate , chemistry , glycine , phosphate , reductase , biocatalysis , ammonia , biochemistry , enzyme , stereochemistry , catalysis , organic chemistry , amino acid , reaction mechanism , arsenic

The highly purified protein C component of clostridial glycine reductase is required in addition to seleno-protein A and protein B for the conversion of glycine to acetate and ammonia in the presence of arsenate. As shown by Arkowitz and Abeles [Arkowitz, R. A. & Abeles, R. H. (1989) Biochemistry 28, 4639-4644], the products are ammonia and acetyl phosphate in the presence of phosphate. The protein C component alone catalyzes an arsenate-dependent decomposition of acetyl phosphate, showing that it serves as the acetyl group acceptor in the overall reaction. A thiol-reducing agent and Mg2+ are required for catalysis of the arsenolysis reaction by protein C. Alkylation or heating at 60 degrees C completely abolishes the ability of protein C to catalyze the arsenolysis reaction and to participate as an essential component in the overall glycine reductase reaction.

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