(Q41924238)

English

Mutation of His465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity toward more alkaline pH.

scientific article published on 21 September 2009

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Mutation of His465 alters the pH-dependent spectroscopic properties of Escherichia coli glutamate decarboxylase and broadens the range of its activity toward more alkaline pH. (English)

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Escherichia coli

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Escherichia coli

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inferred from title

Daniela De Biase

7

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Maurice C. R. Franssen

4

object named as

Maurice C R Franssen

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Europe PubMed Central

PMC publication ID

14 October 2017

author name string

Eugenia Pennacchietti

1

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Tijs M Lammens

2

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Guido Capitani

3

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

Robert A John

5

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Europe PubMed Central

PMC publication ID

14 October 2017

Francesco Bossa

6

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Europe PubMed Central

PMC publication ID

14 October 2017

language of work or name

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publication date

21 September 2009

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Europe PubMed Central

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14 October 2017

Journal of Biological Chemistry

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Europe PubMed Central

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14 October 2017

284

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Europe PubMed Central

PMC publication ID

14 October 2017

46

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

31587-31596

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

A common structural basis for pH- and calmodulin-mediated regulation in plant glutamate decarboxylase

1 reference

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EMBL Nucleotide Sequence Database in 2006.

1 reference

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Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB.

1 reference

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Crystal structure and functional analysis of Escherichia coli glutamate decarboxylase

1 reference

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RevTrans: Multiple alignment of coding DNA from aligned amino acid sequences.

1 reference

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Structural basis of perturbed pKa values of catalytic groups in enzyme active sites

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1 reference

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1 reference

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Mechanisms of acid resistance in enterohemorrhagic Escherichia coli

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A proposed structure for the 330-nm chromophore of glutamate decarboxylase and other pyridoxal 5′-phosphate dependent enzymes

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5 June 2018

Comparison of the absorbance spectra and fluorescence behavior of phosphorylase b with that of model pyridoxal phosphate derivatives in various solvents

1 reference

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5 June 2018

Spectra of 3-hydroxypyridines. Band-shape analysis and evaluation of tautomeric equilibria.

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5 June 2018

pH jump studies of glutamate decarboxylase. Evidence for a pH-dependent conformation change

1 reference

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5 June 2018

Spectroscopic study of the Schiff bases of dodecylamine with pyridoxal 5'-phosphate and 5'-deoxypyridoxal. A model for the Schiff bases of pyridoxal 5'-phosphate in biological systems

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18 August 2018

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18 August 2018

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18 August 2018

The response to stationary-phase stress conditions in Escherichia coli: role and regulation of the glutamic acid decarboxylase system.

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Analysis of the pH- and ligand-induced spectral transitions of tryptophanase: activation of the coenzyme at the early steps of the catalytic cycle

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The Roles of His-167 and His-275 in the Reaction Catalyzed by Glutamate Decarboxylase fromEscherichia coli

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Natural selection promotes the conservation of linkage of co-expressed genes

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Physical-Chemical Studies on the Pyridoxal Phosphate Binding Site in Sodium Borohydride-reduced and Native Phosphorylase

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1 reference

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20 August 2023

Identifiers

10.1074/JBC.M109.049577

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 October 2017

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