The novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8. (Q38331950)

2 September 2017

The novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8. (English)

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2 September 2017

Thermus thermophilus

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Nobe Y

1

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2 September 2017

Kawaguchi S

2

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2 September 2017

Ura H

3

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2 September 2017

Nakai T

4

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2 September 2017

Hirotsu K

5

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2 September 2017

Kato R

6

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2 September 2017

Kuramitsu S

7

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2 September 2017

language of work or name

English

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publication date

1 November 1998

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Journal of Biological Chemistry

2 September 2017

11

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based on heuristic

inferred from page(s)

published in

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2 September 2017

273

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2 September 2017

45

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2 September 2017

29554-29564

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Aminotransferases: demonstration of homology and division into evolutionary subgroups.

2 September 2017

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Isolation and characterization of a gene coding for a novel aspartate aminotransferase from Rhizobium meliloti

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An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8.

21 January 2018

1 reference

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Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases

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Pyridoxal phosphate-dependent enzymes

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Purification and characterization of thermostable aspartate aminotransferase from a thermophilic Bacillus species

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Description of Thermus thermophilus (Yoshida and Oshima) comb. nov., a Nonsporulating Thermophilic Bacterium from a Japanese Thermal Spa

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Cloning and sequencing of aspartate aminotransferase from Thermus aquaticus YT1.

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Cloning and sequencing of the gene coding for aspartate aminotransferase from the thermoacidophilic archaebacterium Sulfolobus solfataricus

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Cloning and nucleotide sequencing of Rhizobium meliloti aminotransferase genes: an aspartate aminotransferase required for symbiotic nitrogen fixation is atypical

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Purification, catalytic properties, and thermal stability of threo-Ds-3-isopropylmalate dehydrogenase coded by leuB gene from an extreme thermophile, Thermus thermophilus strain HB8.

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2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli

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X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase

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Domain closure in mitochondrial aspartate aminotransferase

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

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

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X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from Escherichia coli in three forms

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Crystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9 A resolution

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Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate

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

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Enzyme flexibility: a new concept in recognition of hydrophobic substrates.

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Paracoccus denitrificans aromatic amino acid aminotransferase: a model enzyme for the study of dual substrate recognition mechanism

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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Transaminase activity in human blood

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Protonation state of the active-site Schiff base of aromatic amino acid aminotransferase: modulation by binding of ligands and implications for its role in catalysis.

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PDBsum: a Web-based database of summaries and analyses of all PDB structures

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Improved tools for biological sequence comparison

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

21 January 2018

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Active-site Arg --> Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase.

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

21 January 2018

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Construction of aminotransferase chimeras and analysis of their substrate specificity.

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Replacement of active-site lysine-239 of thermostable aspartate aminotransferase by S-(2-aminoethyl)cysteine: properties of the mutant enzyme.

21 January 2018

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Branched-chain amino acid aminotransferase of Escherichia coli: overproduction and properties.

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Interior and surface of monomeric proteins

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One thousand families for the molecular biologist

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The complete genome sequence of Escherichia coli K-12

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Identifiers

DOI

10.1074/JBC.273.45.29554

1 reference

2 September 2017

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