Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity

doi 10.1021/jacs.7b12045.s010

Full Text

Abstract

Available in

Date

Unknown

Authors

Unknown

Publisher

American Chemical Society (ACS)

Related search

Membrane Allostery and Unique Hydrophobic Sites Promote Enzyme Substrate Specificity

English

Correction: Deconstructing the DGAT1 Enzyme: Membrane Interactions at Substrate Binding Sites

Multidisciplinary

English

Substrate Driven Allostery in a Mitochondrial Cytochrome P450 Enzyme

Biophysical Journal

English

The Novel Human Protein ArginineN-Methyltransferase PRMT6 Is a Nuclear Enzyme Displaying Unique Substrate Specificity

Journal of Biological Chemistry

Molecular Biology

English

Substrate and Inhibitor Specificity of Interleukin-1β-Converting Enzyme and Related Caspases

Journal of Biological Chemistry

Molecular Biology

English

Enzyme Specificity in Reactions of More Than One Co-Substrate

Biochemical Journal

Molecular Biology

English

Carboxypeptidase in Prolyl Oligopeptidase Family: Unique Enzyme Activation and Substrate-Screening Mechanisms

Journal of Biological Chemistry

Molecular Biology

English

The Isolation and Substrate Specificity of a Bovine Kidney Enzyme Cleaving L-Prolylvalylglycine

Biochemical Society Transactions

English

Competition and Allostery Govern Substrate Selectivity of Cyclooxygenase-2

Proceedings of the National Academy of Sciences of the United States of America

Multidisciplinary

English