Mechanism of substrate inactivation of Escherichia coli S-adenosylmethionine decarboxylase
Author:
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi00394a022
Reference19 articles.
1. Escherichia coli S-adenosylmethionine decarboxylase. Subunit structure, reductive amination, and NH2-terminal sequences.
2. The Presence of Covalently Bound Pyruvate in d-Proline Reductase and Its Participation in the Catalytic Process
3. Studies of the mechanism of action of D-proline reductase: The presence on covalently bound pyruvate and its role in the catalytic process
4. Chromatographic analysis of the chiral and covalent instability of S-adenosyl-L-methionine
5. Synthesis and biochemical properties of chemically stable product analogs of the reaction catalyzed by S-adenosyl-L-methionine decarboxylase
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