Aspartate Kinase

"Aspartate Kinase" 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

An enzyme that catalyzes the formation of beta-aspartyl phosphate from aspartic acid and ATP. Threonine serves as an allosteric regulator of this enzyme to control the biosynthetic pathway from aspartic acid to threonine. EC 2.7.2.4.

Descriptor ID

D001222

MeSH Number(s)

D08.811.913.696.630.050

Concept/Terms

Below are MeSH descriptors whose meaning is more general than "Aspartate Kinase".

Chemicals and Drugs [D]
Enzymes and Coenzymes [D08]
Enzymes [D08.811]
Transferases [D08.811.913]
Phosphotransferases [D08.811.913.696]
Phosphotransferases (Carboxyl Group Acceptor) [D08.811.913.696.630]
Aspartate Kinase [D08.811.913.696.630.050]

Below are MeSH descriptors whose meaning is related to "Aspartate Kinase".

Below are MeSH descriptors whose meaning is more specific than "Aspartate Kinase".

Aspartate Kinase
Aspartokinase Homoserine Dehydrogenase

publications

Timeline | Most Recent

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

Bar chart showing 1 publications over 1 distinct years, with a maximum of 1 publications in 1994

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

Year	Major Topic	Minor Topic	Total
1994	1	0	1

Below are the most recent publications written about "Aspartate Kinase" by people in Profiles.

Mechanism of arginine sensing by CASTOR1 upstream of mTORC1. Nature. 2016 08 11; 536(7615):229-33.

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Isolation and characterization of the aspartokinase and aspartate semialdehyde dehydrogenase operon from mycobacteria. Mol Microbiol. 1994 Feb; 11(4):629-39.

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Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase. J Biol Chem. 1993 May 05; 268(13):9448-65.

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Fine-structure mapping of cis-acting control sites in the lysC operon of Bacillus subtilis. FEMS Microbiol Lett. 1992 Apr 01; 71(1):23-7.

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Identification of aecA mutations in Bacillus subtilis as nucleotide substitutions in the untranslated leader region of the aspartokinase II operon. J Gen Microbiol. 1991 May; 137(5):1135-43.

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Desensitization of Bacillus subtilis aspartokinase I to allosteric inhibition by meso-diaminopimelate allows aspartokinase I to function in amino acid biosynthesis during exponential growth. J Bacteriol. 1990 Aug; 172(8):4690-3.

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Comparison of the three aspartokinase isozymes in Bacillus subtilis Marburg and 168. J Bacteriol. 1990 Feb; 172(2):701-8.

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Chromosomal location of the Bacillus subtilis aspartokinase II gene and nucleotide sequence of the adjacent genes homologous to uvrC and trx of Escherichia coli. J Gen Microbiol. 1989 Nov; 135(11):2931-40.

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Mechanism of expression of the overlapping genes of Bacillus subtilis aspartokinase II. J Biol Chem. 1988 Jul 05; 263(19):9526-32.

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J Gen Microbiol
J Biol Chem
J Bacteriol
Mol Microbiol
FEMS Microbiol Lett
Nature