Amino Acid Isomerases

"Amino Acid Isomerases" 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

Enzymes that catalyze either the racemization or epimerization of chiral centers within amino acids or derivatives. EC 5.1.1.

Descriptor ID

D000591

MeSH Number(s)

D08.811.399.894.200

Concept/Terms

Amino Acid Isomerases

Amino Acid Racemases

Below are MeSH descriptors whose meaning is more general than "Amino Acid Isomerases".

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Isomerases [D08.811.399]
Racemases and Epimerases [D08.811.399.894]
Amino Acid Isomerases [D08.811.399.894.200]

Below are MeSH descriptors whose meaning is related to "Amino Acid Isomerases".

Below are MeSH descriptors whose meaning is more specific than "Amino Acid Isomerases".

Amino Acid Isomerases
Alanine Racemase

publications

Timeline | Most Recent

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

Bar chart showing 15 publications over 6 distinct years, with a maximum of 5 publications in 1994

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

Year	Major Topic	Minor Topic	Total
1994	2	3	5
1995	3	0	3
1997	2	2	4
2009	0	1	1
2010	0	1	1
2013	1	0	1

Below are the most recent publications written about "Amino Acid Isomerases" by people in Profiles.

Investigation of the essentiality of glutamate racemase in Mycobacterium smegmatis. J Bacteriol. 2014 Dec; 196(24):4239-44.

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Structural basis for the broad specificity of a new family of amino-acid racemases. Acta Crystallogr D Biol Crystallogr. 2014 Jan; 70(Pt 1):79-90.

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Emerging knowledge of regulatory roles of D-amino acids in bacteria. Cell Mol Life Sci. 2011 Mar; 68(5):817-31.

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D-amino acids govern stationary phase cell wall remodeling in bacteria. Science. 2009 Sep 18; 325(5947):1552-5.

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Substrate recognition and selection by the initiation module PheATE of gramicidin S synthetase. J Am Chem Soc. 2001 Nov 14; 123(45):11208-18.

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Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases. Biochemistry. 2001 Jun 19; 40(24):7099-108.

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Kinetic analysis of three activated phenylalanyl intermediates generated by the initiation module PheATE of gramicidin S synthetase. Biochemistry. 2001 May 08; 40(18):5329-37.

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Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase. Biochemistry. 2000 May 16; 39(19):5775-87.

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Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis. Science. 1999 Apr 16; 284(5413):486-9.

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Sequence-specific and phosphorylation-dependent proline isomerization: a potential mitotic regulatory mechanism. Science. 1997 Dec 12; 278(5345):1957-60.

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