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Crystal Structure of a D-Amino Acid Aminotransferase: How the Protein Controls Stereoselectivity

Data up to Jan 2025

Published1995
Citations152
References28

Total Citations Per Year

Abstract

References (28)

Solvent content of protein crystals

1968 • 7,954 citations

Crystallographic R Factor Refinement by Molecular Dynamics

1987 • 1,982 citations

Atomic structure of the actin: DNase I complex

1990 • 1,897 citations

A graphics model building and refinement system for macromolecules

1978 • 1,858 citations

Resolution of phase ambiguity in macromolecular crystallography

1985 • 1,040 citations

Selection of representative protein data sets

1992 • 823 citations

The SWISS-PROT protein sequence data bank

1992 • 530 citations

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

1984 • 470 citations

Methods and programs for direct-space exploitation of geometric redundancies

1976 • 383 citations

Structural changes in glycogen phosphorylase induced by phosphorylation

1988 • 302 citations

Dialkylglycine Decarboxylase Structure: Bifunctional Active Site and Alkali Metal Sites

1993 • 189 citations

Generalized method of determining heavy-atom positions using the difference Patterson function

1987 • 139 citations

Three-dimensional structure of tyrosine phenol-lyase

1993 • 130 citations

Thermostable D-amino acid aminotransferase from a thermophilic Bacillus species

1989 • 92 citations

Crystal structure of true enzymic reaction intermediates: Aspartate and glutamate ketimines in aspartate aminotransferase

1993 • 79 citations

The primary structure of thermostable D-amino acid aminotransferase from a thermophilic Bacillus species and its correlation with L-amino acid aminotransferases

1989 • 79 citations

The tyrosine-225 to phenylalanine mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both kcat and Km

1991 • 71 citations

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

1994 • 47 citations

Unique stereospecificity of D-amino acid aminotransferase and branched-chain L-amino acid aminotransferase for C-4' hydrogen transfer of the coenzyme

1993 • 44 citations

Tyr225 in Aspartate Aminotransferase: Contribution of the Hydrogen Bond between Tyr225 and Coenzyme to the Catalytic Reaction1

1991 • 40 citations

Use of the multiwire area detector diffractometer as a national resource for protein crystallography

1985 • 39 citations

[ON THE BIOLOGICAL ROLE OF CARNOSINE].

1963 • 37 citations

The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E.coli

1994 • 33 citations

Purification and crystallization of D‐amino acid aminotransferase of Bacillus sphaericus

1974 • 27 citations

Site-directed mutagenesis of the cysteinyl residues and the active-site serine residue of bacterial D-amino acid transaminase

1989 • 25 citations

Structure of the complex between pyridoxal 5'-phosphate and the tyrosine 225 to phenylalanine mutant of Escherichia coli aspartate aminotransferase determined by isotope-edited classical Raman difference spectroscopy

1993 • 17 citations

Preliminary X-ray data for a d-amino acid amino-transferase from a novel thermophilic Bacillus

1987 • 16 citations

Reconstitution of D‐amino acid aminotransferase

1975 • 9 citations

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Crystal Structure of a D-Amino Acid Aminotransferase: How the Protein Controls… (1995) – Biochemistry | Metascience Observatory Explorer