Insights into the Mechanism of Pseudomonas dacunhae Aspartate β-Decarboxylase from Rapid-Scanning Stopped-Flow Kinetics
Author:
Affiliation:
1. Department of Chemistry, University of Georgia, Athens, Georgia 30602
2. Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi100272g
Reference29 articles.
1. Identification of mammalian aspartate-4-decarboxylase
2. Plasmid-Encoded asp Operon Confers a Proton Motive Metabolic Cycle Catalyzed by an Aspartate-Alanine Exchange Reaction
3. The Crystal Structure of the Pseudomonas dacunhae Aspartate-β-Decarboxylase Dodecamer Reveals an Unknown Oligomeric Assembly for a Pyridoxal-5′-Phosphate-Dependent Enzyme
4. Structure, Assembly, and Mechanism of a PLP-Dependent Dodecameric l-Aspartate β-Decarboxylase
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5. Structure-guided engineering ofPseudomonas dacunhael-aspartate β-decarboxylase forl-homophenylalanine synthesis;Chemical Communications;2020
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