Evidence for presence of an arginine residue in the coenzyme A binding site of choline acetyltransferase. | Zendy

Henry G. Mautner | Zendy; A A Pakula | Zendy; Robert E. Merrill | Zendy

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Evidence for presence of an arginine residue in the coenzyme A binding site of choline acetyltransferase.

Author(s) -

Henry G. Mautner,

A A Pakula,

Robert E. Merrill

Publication year - 1981

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.78.12.7449

Subject(s) - phenylglyoxal , arginine , chemistry , biochemistry , choline acetyltransferase , acetyltransferase , reagent , choline , residue (chemistry) , nad+ kinase , enzyme , sodium , stereochemistry , amino acid , biology , acetylation , acetylcholine , organic chemistry , gene , endocrinology

Choline acetyltransferase (acetyl-CoA:choline O-acetyltransferase, EC 2.3.1.6) may be inactivated by arginine-specific reagents such as butanedione, phenylglyoxal, and camphorquinone-10-sulfonic acid. The enantiomers of the latter compound were prepared, but inactivation was not stereospecific. Protection against inactivation by the arginine-specific reagents was provided by CoA and, to a lesser extent, by 3'-dephospho-CoA. No protection was provided by choline, NAD+, NADH, NADP+, or NADPH. Sodium chloride could protect, to some extent, against inactivation by arginine-specific reagents; this protection showed no cation or anion specificity. The data are compatible with the postulate that the salt anion competes with the attachment of the 3'-phospho group of CoA to an active site arginine residue.

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