(Q47798817)

5 February 2018

title

Kinetic properties and thermal stabilities of mutant forms of mitochondrial aspartate aminotransferase. (English)

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5 February 2018

author

Sergio Giannattasio

3

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5 February 2018

author name string

A Azzariti

1

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5 February 2018

R A Vacca

2

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5 February 2018

R S Merafina

4

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5 February 2018

E Marra

5

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5 February 2018

S Doonan

6

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5 February 2018

publication date

1 July 1998

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5 February 2018

Biochimica et Biophysica Acta

published in

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5 February 2018

volume

1386

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5 February 2018

issue

1

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5 February 2018

page(s)

29-38

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5 February 2018

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

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

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7 January 2021

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

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7 January 2021

The three-dimensional structure of mitochondrial aspartate aminotransferase at 4.5 Å resolution

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7 January 2021

The open/closed conformational equilibrium of aspartate aminotransferase. Studies in the crystalline state and with a fluorescent probe in solution

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7 January 2021

Domain closure in mitochondrial aspartate aminotransferase

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7 January 2021

Import of mutant forms of mitochondrial aspartate aminotransferase into isolated mitochondria

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7 January 2021

The in vitro-synthesized precursor and mature mitochondrial aspartate aminotransferase share the same import pathway in isolated mitochondria

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7 January 2021

Precursor of mitochondrial aspartate aminotransferase synthesized in Escherichia coli is complexed with heat-shock protein DnaK

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7 January 2021

Shift in pH-rate profile and enhanced discrimination between dicarboxylic and aromatic substrates in mitochondrial aspartate aminotransferase Y70H.

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Transaminase activity in human blood

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7 January 2021

Mitochondrial aspartate transaminase. II. Isolation and characterization of the multiple forms.

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KINETIC STUDIES OF GLUTAMIC OXALOACETIC TRANSAMINASE ISOZYMES.

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Substitution of apolar residues in the active site of aspartate aminotransferase by histidine. Effects on reaction and substrate specificity

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7 January 2021

The site of binding of pyridoxal-5'-phosphate to heart glutamic-aspartic transaminase

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7 January 2021

Comparison of aspartate aminotransferase with other aminotransferases by absorption-spectrum analysis

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7 January 2021

The roles of Tyr70 and Tyr225 in aspartate aminotransferase assessed by analysing the effects of mutations on the multiple reactions of the substrate analogue serine o-sulphate

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7 January 2021

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

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7 January 2021

A comparative study of the thermal inactivation of cytosolic and mitochondrial aspartate aminotransferases

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7 January 2021

Limited proteolysis as a probe of conformational changes in aspartate aminotransferase from Sulfolobus solfataricus

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7 January 2021

10.1016/S0167-4838(98)00057-0

Identifiers

DOI

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5 February 2018

PubMed ID

9675237

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5 February 2018