Reaction of the adenine nucleotide analogue 5'-p-fluorosulfonylbenzoyl adenosine at distinct tyrosine and cysteine residues of rabbit muscle pyruvate kinase.-Reference-Cited by-同舟云学术

Reaction of the adenine nucleotide analogue 5'-p-fluorosulfonylbenzoyl adenosine at distinct tyrosine and cysteine residues of rabbit muscle pyruvate kinase.

Published:1981-10 Issue:20 Volume:256 Page:10276-10283
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Annamalai A.E.,Colman R.F.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference41 articles.

1. Chromium(III)-adenosine triphosphate as a paramagnetic probe to determine intersubstrate distances on pyruvate kinase. Detection of an active enzyme-metal-ATP-metal complex.

2. Arrangement and conformations of substrates at the active site of pyruvate kinase from model building studies based on magnetic resonance data.

3. Structures of enzyme-bound metal-nucleotide complexes in the phosphoryl transfer reaction of muscle pyruvate kinase. 31P NMR studies with magnesium and kinetic studies with chromium nucleotides.

4. Magnetic resonance and kinetic studies of the spatial arrangement of phosphoenolpyruvate and chromium (III)-adenosine diphosphate at the catalytic site of pyruvate kinase.

5. 31P NMR studies of enzyme-bound substrates of rabbit muscle pyruvate kinase. Equilibrium constants, exchange rates, and NMR parameters.

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