Investigation of the catalytic site within the ATP-grasp domain of Clostridium symbiosum pyruvate phosphate dikinase (Q27633437)

2

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M McGuire

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K Huang

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G Kapadia

5

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O Herzberg

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B M Martin

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D Dunaway-Mariano

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

5 October 2001

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published in

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volume

276

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issue

40

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page(s)

37630-9

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cites work

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Location of the phosphate binding site within Clostridium symbiosum pyruvate phosphate dikinase

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Molecular structure of Escherichia coli PurT-encoded glycinamide ribonucleotide transformylase

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Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase

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Location of the catalytic site for phosphoenolpyruvate formation within the primary structure of Clostridium symbiosum pyruvate phosphate dikinase. 2. Site-directed mutagenesis of an essential arginine contained within an apparent P-loop.

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D-alanine:D-alanine ligase: phosphonate and phosphinate intermediates with wild type and the Y216F mutant

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Movement of the biotin carboxylase B-domain as a result of ATP binding

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Kinetic evidence for separate site catalysis by pyruvate phosphate dikinase

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Substrate binding domains in pyruvate phosphate dikinase

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Energetics of pyruvate phosphate dikinase catalysis

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Determination of the Nucleotide Binding Site withinClostridium symbiosumPyruvate Phosphate Dikinase by Photoaffinity Labeling, Site-Directed Mutagenesis, and Structural Analysis†

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Identifiers

DOI

10.1074/JBC.M105631200

1 reference

Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

11468288

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Consolidated OpenCitations Corpus – April 2017