(Q27622224)

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Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate

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scholarly article

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Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate (English)

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crystal structure

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Bacillus stearothermophilus

object named as

Bacillus stearothermophilus

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based on heuristic

inferred from title

3

object named as

P Setlow

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author name string

M J Jedrzejas

1

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M Chander

2

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G Krishnasamy

4

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language of work or name

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publication date

28 July 2000

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Journal of Biological Chemistry

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275

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23146-53

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30

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Phylogeny and ontogeny of the phosphoglycerate mutases—IV. Distribution of glycerate-2,3-P2 dependent and independent phosphoglycerate mutases in algae, fungi, plants and animals

1 reference

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21 January 2018

Structure and mechanism of action of a novel phosphoglycerate mutase from Bacillus stearothermophilus

1 reference

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21 January 2018

The internal pH of the forespore compartment of Bacillus megaterium decreases by about 1 pH unit during sporulation

1 reference

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Analysis of the relationship between the decrease in pH and accumulation of 3-phosphoglyceric acid in developing forespores of Bacillus species

1 reference

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21 January 2018

The 2.3 A X-ray crystal structure of S. cerevisiae phosphoglycerate mutase

1 reference

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Phosphoglycerate mutase from wheat germ: studies with isotopically labeled 3-phospho-D-glycerates showing that the catalyzed reaction is intramolecular. Appendix: Phosphoglycerate mutase from wheat germ: isolation, crystallization, and properties

1 reference

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21 January 2018

A superfamily of metalloenzymes unifies phosphopentomutase and cofactor-independent phosphoglycerate mutase with alkaline phosphatases and sulfatases

1 reference

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21 January 2018

The geometry of metal-ligand interactions relevant to proteins.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

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Structure and mechanism of alkaline phosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

21 January 2018

Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102

1 reference

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21 January 2018

Structural studies on a 2,3-diphosphoglycerate independent phosphoglycerate mutase from Bacillus stearothermophilus.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

21 January 2018

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

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Solvent content of protein crystals

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

21 January 2018

PROCHECK: a program to check the stereochemical quality of protein structures

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

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Improved methods for building protein models in electron density maps and the location of errors in these models

1 reference

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Analysis and prediction of structural motifs in the glycolytic enzymes

1 reference

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Hard and Soft Acids and Bases

1 reference

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Catalysis by metal-activated hydroxide in zinc and manganese metalloenzymes

1 reference

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Structural chemistry and biology of manganese metalloenzymes

1 reference

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Do metal ions promote the re-activation of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutases?

1 reference

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21 January 2018

Searching protein structure databases has come of age.

1 reference

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21 January 2018

Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis

1 reference

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21 January 2018

Stereochemistry of phosphoryl group transfer using a chiral [16O, 17O, 18O] stereochemical course of alkaline phosphatase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

21 January 2018

The two analogous phosphoglycerate mutases of Escherichia coli

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

21 January 2018

Cooperative manganese (II) activation of 3-phosphoglycerate mutase of Bacillus megaterium: a biological pH-sensing mechanism in bacterial spore formation and germination

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

21 January 2018

Isozymes of phosphoglyceromutase from the developing endosperm of Ricinus communis: isolation and kinetic properties

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

21 January 2018

Wheat germ phosphoglycerate mutase: evidence for a metalloenzyme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

21 January 2018

Refined structure of alkaline phosphatase from Escherichia coli at 2.8 A resolution

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M002544200

21 January 2018

Identifiers

10.1074/JBC.M002544200

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