A covalently bound catalytic intermediate in Escherichia coli asparaginase: crystal structure of a Thr-89-Val mutant (Q27733238)

2

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C Derst

3

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S Schleper

4

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K H Röhm

5

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A Wlodawer

The 18O isotope effect in 13C nuclear magnetic resonance spectroscopy: mechanistic studies on asparaginase from Escherichia coli

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language of work or name

English

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publication date

22 July 1996

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published in

FEBS Letters

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volume

390

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page(s)

211-6

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issue

2

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cites work

1 reference

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Refined crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase.

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Structural characterization of Pseudomonas 7A glutaminase-asparaginase

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Proteasome from Thermoplasma acidophilum: a threonine protease

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Three-dimensional structure of human lysosomal aspartylglucosaminidase

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A protein catalytic framework with an N-terminal nucleophile is capable of self-activation

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

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Interaction between L-aspartic acid and L-asparaginase from Escherichia coli: binding and inhibition studies.

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Accurate bond and angle parameters for X-ray protein structure refinement

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Glutaminase-free asparaginase from vibrio succinogenes: an antilymphoma enzyme lacking hepatotoxicity

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Amino acid sequence of the diazooxonorleucine binding site of Acinetobacter and Pseudomonas 7 A glutaminase-asparaginase enzymes

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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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A left-handed crossover involved in amidohydrolase catalysis. Crystal structure of Erwinia chrysanthemi L-asparaginase with bound L-aspartate

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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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Phosphocholine binding immunoglobulin Fab McPC603. An X-ray diffraction study at 2.7 A

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Divalent cation binding to the high- and low-affinity sites on G-actin

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10.1016/0014-5793(96)00660-6

21 January 2018

Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

2640364

OpenCitations bibliographic resource ID

2640364

1 reference