D-Alanine Transaminase

"D-Alanine Transaminase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure, which enables searching at various levels of specificity.

MeSH information

Definition | Details | More General Concepts | Related Concepts | More Specific Concepts

A PYRIDOXAL PHOSPHATE containing enzyme that catalyzes the reversible transfer of an amino group between D-Alanine and alpha-ketoglutarate to form PYRUVATE and D-GLUTAMATE, respectively. It plays a role in the synthesis of the bacterial CELL WALL. This enzyme was formerly classified as EC 2.6.1.10.

Descriptor ID

D051263

MeSH Number(s)

D08.811.913.477.700.347

Concept/Terms

D-Alanine Transaminase

Below are MeSH descriptors whose meaning is more general than "D-Alanine Transaminase".

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Transferases [D08.811.913]
Nitrogenous Group Transferases [D08.811.913.477]
Transaminases [D08.811.913.477.700]
D-Alanine Transaminase [D08.811.913.477.700.347]

Below are MeSH descriptors whose meaning is related to "D-Alanine Transaminase".

Below are MeSH descriptors whose meaning is more specific than "D-Alanine Transaminase".

publications

Timeline | Most Recent

This graph shows the total number of publications written about "D-Alanine Transaminase" by people in Harvard Catalyst Profiles by year, and whether "D-Alanine Transaminase" was a major or minor topic of these publication.

Bar chart showing 5 publications over 3 distinct years, with a maximum of 2 publications in 1995 and 1998

To see the data from this visualization as text, click here.

Year	Minor Topic	Total
1995	2	2
1996	1	1
1998	2	2

Below are the most recent publications written about "D-Alanine Transaminase" by people in Profiles.

Effects of the E177K mutation in D-amino acid transaminase. Studies on an essential coenzyme anchoring group that contributes to stereochemical fidelity. Biochemistry. 1999 Jan 26; 38(4):1323-31.

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Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination. Protein Eng. 1998 Aug; 11(8):613-9.

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Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase. Biochemistry. 1998 Apr 07; 37(14):4958-67.

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Substrate inhibition of D-amino acid transaminase and protection by salts and by reduced nicotinamide adenine dinucleotide: isolation and initial characterization of a pyridoxo intermediate related to inactivation. Biochemistry. 1998 Mar 03; 37(9):2879-88.

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Interaction of pyridoxal 5'-phosphate with tryptophan-139 at the subunit interface of dimeric D-amino acid transaminase. Biochemistry. 1996 Feb 20; 35(7):2112-6.

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Catalytic ability and stability of two recombinant mutants of D-amino acid transaminase involved in coenzyme binding. Protein Sci. 1995 Dec; 4(12):2578-86.

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Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity. Biochemistry. 1995 Aug 01; 34(30):9661-9.

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Staphylococcus haemolyticus contains two D-glutamic acid biosynthetic activities, a glutamate racemase and a D-amino acid transaminase. J Bacteriol. 1995 Jan; 177(2):336-42.

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Determination of free D-amino acids with a bacterial transaminase: their depletion leads to inhibition of bacterial growth. Anal Biochem. 1994 Apr; 218(1):204-9.

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Role reversal for substrates and inhibitors. Slow inactivation of D-amino acid transaminase by its normal substrates and protection by inhibitors. J Biol Chem. 1993 Aug 25; 268(24):17687-94.

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