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Kinetic evidence of a noncatalytic substrate binding site that regulates activity in legionella pneumophila l -serine dehydratase
Gregory A. Grant
Division of Dermatology
Department of Developmental Biology
Roy and Diana Vagelos Division of Biology & Biomedical Sciences (DBBS)
Institute of Clinical and Translational Sciences (ICTS)
DBBS - Molecular Cell Biology
Research output
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Contribution to journal
›
Article
›
peer-review
10
Scopus citations
Overview
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Dive into the research topics of 'Kinetic evidence of a noncatalytic substrate binding site that regulates activity in legionella pneumophila l -serine dehydratase'. Together they form a unique fingerprint.
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Keyphrases
Conformational Change
100%
Legionella Pneumophila
100%
Non-catalytic
100%
Substrate Binding Site
100%
D-Serine Dehydratase
100%
Glyceraldehyde-3-phosphate Dehydrogenase
75%
Noncatalytic Sites
50%
Mycobacterium Tuberculosis (M. tb)
25%
Sequence Homology
25%
Bacterial Cells
25%
Catalytic Activity
25%
Kinetic Analysis
25%
Steady-state Kinetics
25%
Overall Effect
25%
Catalytic Cycle
25%
Catalytic Center
25%
Structural Homology
25%
Fe-S
25%
ACT Domain
25%
Biochemistry, Genetics and Molecular Biology
Binding Site
100%
Legionella pneumophila
100%
Dehydratase
100%
Serine
100%
Conformational Change
36%
Phosphoglycerate Dehydrogenase
27%
Enzyme
18%
Steady State
9%
Sequence Homology
9%
Kinetics
9%
Mycobacterium Tuberculosis
9%
Structural Homology
9%
Enzymatic Activity
9%