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Article

The bifunctional active site of s-adenosylmethionine synthetase. Roles of the active site aspartates.

The Journal of biological chemistry - 12 Nov 1999

Taylor J C, Markham G D

Abstract excerpt

S-Adenosylmethionine (AdoMet) synthetase catalyzes the biosynthesis of AdoMet in a unique enzymatic reaction. Initially the sulfur of methionine displaces the intact tripolyphosphate chain (PPP(i)) from ATP, and subsequently PPP(i) is hydrolyzed to PP(i) and P(i) before product release. The crystal structure of Escherichia coli AdoMet synthetase shows that the active site contains four aspartate residues....

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Source

Identifiers

PMID: 10551856
DOI: 10.1074/jbc.274.46.32909

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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