(Q42844917)

English

The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases

scientific article published on September 1995

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Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases (English)

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

Escherichia coli

1 reference

based on heuristic

inferred from title

author name string

J J Onuffer

1

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

B T Ton

2

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

I Klement

3

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

J F Kirsch

4

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

publication date

1 September 1995

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

Protein Science

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

4

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

9

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

1743-1749

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Crystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Mechanism of action of aspartate aminotransferase proposed on the basis of its spatial structure

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Measurement of protein by spectrophotometry at 205 nm.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Nonidentity of the aspartate and the aromatic aminotransferase components of transaminase A in Escherichia coli.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Aromatic amino acid aminotransferase of Escherichia coli: nucleotide sequence of the tyrB gene

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

[21] Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Role of arginine-292 in the substrate specificity of aspartate aminotransferase as examined by site-directed mutagenesis.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Kinetic isotope effect studies on aspartate aminotransferase: evidence for a concerted 1,3 prototropic shift mechanism for the cytoplasmic isozyme and L-aspartate and dichotomy in mechanism.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Brønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

The Purification and Properties of the Aspartate Aminotransferase and Aromatic-Amino-Acid Aminotransferase from Escherichia coli

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Mapping of the aspartate and aromatic amino acid aminotransferase genes tyrB and aspC

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Effects of replacement of tryptophan-140 by phenylalanine or glycine on the function of Escherichia coli aspartate aminotransferase.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Three-dimensional structures of aspartate aminotransferase from Escherichia coli and its mutant enzyme at 2.5 A resolution.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Computational approach towards the three-dimensional structure of E. coli tyrosine aminotransferase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

27 May 2018

Characterization of the apparent negative co-operativity induced in Escherichia coli aspartate aminotransferase by the replacement of Asp222 with alanine. Evidence for an extremely slow conformational change

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2143219

16 August 2018

Transamination of aromatic amino acids in Escherichia coli

1 reference

https://pubmed.ncbi.nlm.nih.gov/8528072

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

[Arg292----Val] or [Arg292----Leu] mutation enhances the reactivity of Escherichia coli aspartate aminotransferase with aromatic amino acids

1 reference

https://pubmed.ncbi.nlm.nih.gov/8528072

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Modeling the three-dimensional structures of bacterial aminotransferases

1 reference

https://pubmed.ncbi.nlm.nih.gov/8528072

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Evolutionary relationships among aminotransferases. Tyrosine aminotransferase, histidinol-phosphate aminotransferase, and aspartate aminotransferase are homologous proteins

1 reference

https://pubmed.ncbi.nlm.nih.gov/8528072

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Reversible dissociation and unfolding of aspartate aminotransferase from Escherichia coli: characterization of a monomeric intermediate

1 reference

https://pubmed.ncbi.nlm.nih.gov/8528072

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Pre-steady-state kinetics of Escherichia coli aspartate aminotransferase catalyzed reactions and thermodynamic aspects of its substrate specificity

1 reference

https://pubmed.ncbi.nlm.nih.gov/8528072

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Dexamethasone phosphate-induced synthesis of tyrosine aminotransferase in hepatoma tissue culture cells. Studies of the early phases of induction and of the steroid requirement for maintanance of the induced rate of synthesis

1 reference

https://pubmed.ncbi.nlm.nih.gov/8528072

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase

1 reference

https://pubmed.ncbi.nlm.nih.gov/8528072

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Specific synthesis of DNA in vitro via a polymerase-catalyzed chain reaction

1 reference

https://pubmed.ncbi.nlm.nih.gov/8528072

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1002/PRO.5560040909

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

8 November 2017

ResearchGate publication ID

0 references

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