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Do bacterial L-asparaginases utilize a catalytic triad Thr-Tyr-Glu?
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title
Do bacterial L-asparaginases utilize a catalytic triad Thr-Tyr-Glu?
(English)
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author name string
K Aghaiypour
series ordinal
1
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A Wlodawer
series ordinal
2
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J Lubkowski
series ordinal
3
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language of work or name
English
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publication date
17 December 2001
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published in
Biochimica et Biophysica Acta
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volume
1550
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issue
2
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page(s)
117-28
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cites work
A new L-asparaginase with antitumour activity?
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7 January 2021
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Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy
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A left-handed crossover involved in amidohydrolase catalysis. Crystal structure of Erwinia chrysanthemi L-asparaginase with bound L-aspartate
1 reference
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The 18O isotope effect in 13C nuclear magnetic resonance spectroscopy: mechanistic studies on asparaginase from Escherichia coli
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Refined crystal structure of Acinetobacter glutaminasificans glutaminase-asparaginase.
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Crystal structure and amino acid sequence of Wolinella succinogenes L-asparaginase
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reference URL
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Structural basis for the activity and substrate specificity of Erwinia chrysanthemi L-asparaginase
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Structural characterization of Pseudomonas 7A glutaminase-asparaginase
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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
1 reference
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reference URL
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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
1 reference
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reference URL
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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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Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups
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Dynamics of a mobile loop at the active site of Escherichia coli asparaginase
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States and functions of tyrosine residues in Escherichia coli asparaginase II.
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Physical properties and subunit structure of l-asparaginase isolated from Erwinia carotovora
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Processing of X-ray diffraction data collected in oscillation mode
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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
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Electron-density map interpretation
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Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
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Accurate bond and angle parameters for X-ray protein structure refinement
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PROCHECK: a program to check the stereochemical quality of protein structures
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WHAT IF: a molecular modeling and drug design program
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The three-dimensional structure of Asn102 mutant of trypsin: role of Asp102 in serine protease catalysis
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The catalytic role of the active site aspartic acid in serine proteases
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Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
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Identifiers
DOI
10.1016/S0167-4838(01)00270-9
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PubMed publication ID
11755201
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ResearchGate publication ID
11602719
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