The Mechanism of the Amidases: MUTATING THE GLUTAMATE ADJACENT TO THE CATALYTIC TRIAD INACTIVATES THE ENZYME DUE TO SUBSTRATE MISPOSITIONING (Q27679688)

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English	The Mechanism of the Amidases: MUTATING THE GLUTAMATE ADJACENT TO THE CATALYTIC TRIAD INACTIVATES THE ENZYME DUE TO SUBSTRATE MISPOSITIONING	scientific article

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7 March 2020

The mechanism of the amidases: mutating the glutamate adjacent to the catalytic triad inactivates the enzyme due to substrate mispositioning (English)

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7 March 2020

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7 March 2020

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7 March 2020

Gerhard A. Venter

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7 March 2020

James C Gumbart

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James C Gumbart

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7 March 2020

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Brandon W Weber

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7 March 2020

Serah W Kimani

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7 March 2020

Arvind Varsani

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7 March 2020

B Trevor Sewell

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14 August 2013

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7 March 2020

Journal of Biological Chemistry

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7 March 2020

288

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7 March 2020

28514-28523

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7 March 2020

Structural insights into the catalytic active site and activity of human Nit2/ω-amidase: kinetic assay and molecular dynamics simulation

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20 March 2017

Unique Aliphatic Amidase from a Psychrotrophic and Haloalkaliphilic Nesterenkonia Isolate

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20 March 2017

Crystallographic analysis of a thermoactive nitrilase

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20 March 2017

Structure of amidase from Pseudomonas aeruginosa showing a trapped acyl transfer reaction intermediate state

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20 March 2017

Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad

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20 March 2017

The nitrilase superfamily: classification, structure and function

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20 March 2017

Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases

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Features and development of Coot

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Refinement of macromolecular structures by the maximum-likelihood method

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UCSF Chimera--a visualization system for exploratory research and analysis

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The finer things in X-ray diffraction data collection

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20 March 2017

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29 September 2017

Improved R-factors for diffraction data analysis in macromolecular crystallography

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20 March 2017

Development and testing of a general amber force field

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7 April 2017

A point-charge force field for molecular mechanics simulations of proteins based on condensed-phase quantum mechanical calculations

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Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density

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7 April 2017

Biochemical and mutational studies of the Bacillus cereus CECT 5050T formamidase support the existence of a C-E-E-K tetrad in several members of the nitrilase superfamily.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3789952

29 September 2017

Identification of the putative tumor suppressor Nit2 as omega-amidase, an enzyme metabolically linked to glutamine and asparagine transamination

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Microbial nitrilases: versatile, spiral forming, industrial enzymes

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29 September 2017

Primary or secondary? Versatile nitrilases in plant metabolism

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29 September 2017

The quaternary structure of the amidase from Geobacillus pallidus RAPc8 is revealed by its crystal packing

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29 September 2017

Molecular analysis of the nitrile catabolism operon of the thermophile Bacillus pallidus RAPc8.

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29 September 2017

A new family of carbon-nitrogen hydrolases

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29 September 2017

The estimation of ammonia using the indophenol blue reaction

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2 June 2018

Structural Basis for Catalysis and Substrate Specificity of Agrobacterium radiobacter N-Carbamoyl-D-amino Acid Amidohydrolase

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21 January 2018

A novel thermostable nitrilase superfamily amidase from Geobacillus pallidus showing acyl transfer activity

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21 January 2018

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27 November 2018

Structure of an aliphatic amidase fromGeobacillus pallidusRAPc8

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Detection of covalent enzyme-substrate complexes of nitrilase by ion-spray mass spectroscopy

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Comparison of cyanide-degrading nitrilases

1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1074/JBC.M113.503284

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Europe PubMed Central

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7 March 2020

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7 March 2020

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Europe PubMed Central

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7 March 2020

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