Dynamics of a mobile loop at the active site of Escherichia coli asparaginase (Q73040236)

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31 October 2019

title

Dynamics of a mobile loop at the active site of Escherichia coli asparaginase (English)

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31 October 2019

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H P Aung

1

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31 October 2019

M Bocola

series ordinal

2

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31 October 2019

S Schleper

series ordinal

3

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31 October 2019

K H Röhm

series ordinal

4

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31 October 2019

language of work or name

English

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publication date

1 September 2000

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Biochimica et Biophysica Acta

31 October 2019

published in

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31 October 2019

volume

1481

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31 October 2019

issue

2

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31 October 2019

page(s)

349-359

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31 October 2019

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Catalytic triads and their relatives

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A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant

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Ion binding induces closed conformation in Pseudomonas 7A glutaminase-asparaginase (PGA): crystal structure of the PGA-SO4(2-)-NH4+ complex at 1.7 A resolution

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On the role of histidine and tyrosine residues in E. coli asparaginase. Chemical modification and 1H-nuclear magnetic resonance studies

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Site-specific mutagenesis of Escherichia coli asparaginase II. None of the three histidine residues is required for catalysis

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States and functions of tyrosine residues in Escherichia coli asparaginase II.

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Probing the role of threonine and serine residues of E. coli asparaginase II by site-specific mutagenesis

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Construction of expression systems for Escherichia coli asparaginase II and two-step purification of the recombinant enzyme from periplasmic extracts

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7 January 2021

Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM--a flexible, portable system.

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pH dependence of the kinetic parameters of l-asparaginase

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A catalytic role for threonine-12 of E. coli asparaginase II as established by site-directed mutagenesis

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7 January 2021

The pH dependence and quenching of the fluorescence of asparaginase from Escherichia coli B

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The use of genetically engineered tryptophan to identify the movement of a domain of B. stearothermophilus lactate dehydrogenase with the process which limits the steady-state turnover of the enzyme

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Detection and characterization of intermediates in the folding of large proteins by the use of genetically inserted tryptophan probes.

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Toward understanding tryptophan fluorescence in proteins

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Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu

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7 January 2021

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Identifiers

DOI

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31 October 2019

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