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Journal ArticleDOI

Mechanisms of signaling and related enzymes

Albert S. Mildvan
- 01 Dec 1997 - 
- Vol. 29, Iss: 4, pp 401-416
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TLDR
From kinetic studies of mutant and metal ion substituted enzymes, the catalytic powers of cell signaling and related enzymes can be rationalized quantitatively by factors contributed by metal ion catalysis (≥105), general acid catalysis, general baseCatalysis, and transition‐state stabilization by cationic and hydrogen bond donating residues (≈103±1).
Citations
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How Enzymes Work: Analysis by Modern Rate Theory and Computer Simulations

TL;DR: A framework for understanding the effects of lowering of the activation free energy and changes in the generalized transmission coefficient on enzyme catalysis is presented, and the contributions of the different factors are identified and quantified by computer simulations.
Journal ArticleDOI

The ABC transporter structure and mechanism: perspectives on recent research

TL;DR: This review examines the recent structural data concerning ABC transporters and related proteins in the light of other experimental and theoretical data, and discusses these data in relation to current ideas concerning thetransporters’ molecular mechanism.
References
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Journal ArticleDOI

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.

TL;DR: The crystal structure of bovine mitochondrial F1-ATPase determined at 2.8 Å resolution supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant.
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The 2.0 Å crystal structure of a heterotrimeric G protein

TL;DR: The structure of a heterotrimeric G protein reveals the mechanism of the nucleotide-dependent engagement of the α and βγ subunits that regulates their interaction with receptor and effector molecules.
Journal ArticleDOI

A general two-metal-ion mechanism for catalytic RNA

TL;DR: The mechanism postulates that chemical catalysis is facilitated by two divalent metal ions 3.9 A apart, as in phosphoryl transfer reactions catalyzed by protein enzymes, such as the 3',5'-exonuclease of Escherichia coli DNA polymerase I.
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Crystal structure of the tyrosine kinase domain of the human insulin receptor.

TL;DR: The structure reveals the determinants of substrate preference for tyrosine rather than serine or threonine and a novel autoinhibition mechanism whereby one of the tyrosines that is autophosphorylated in response to insulin, Tyr 1,162, is bound in the active site.
Journal ArticleDOI

Structure of a Peptide Inhibitor Bound to the Catalytic Subunit of Cyclic Adenosine Monophosphate-Dependent Protein Kinase

TL;DR: The structure of a 20-amino acid peptide inhibitor bound to the catalytic subunit of cyclic AMP-dependent protein kinase, and its interactions with the enzyme, are described and the x-ray crystal structure of the complex is the basis of the analysis.