L,L-diaminopimelate aminotransferase | |||||||||
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Identifiers | |||||||||
EC no. | 2.6.1.83 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a L,L-diaminopimelate aminotransferase (EC 2.6.1.83) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are LL-2,6-diaminoheptanedioate and 2-oxoglutarate, whereas its 3 products are (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate, L-glutamate, and H2O.
This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is LL-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase. Other names in common use include LL-diaminopimelate transaminase, LL-DAP aminotransferase, and LL-DAP-AT. This enzyme participates in lysine biosynthesis.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2Z1Z and 2Z20.
In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.
In enzymology, a diaminopimelate dehydrogenase (EC 1.4.1.16) is an enzyme that catalyzes the chemical reaction
In enzymology, a diaminopimelate epimerase is an enzyme that catalyzes the chemical reaction
The enzyme diaminopimelate decarboxylase (EC 4.1.1.20) catalyzes the cleavage of carbon-carbon bonds in meso 2,6 diaminoheptanedioate to produce CO2 and L-lysine, the essential amino acid. It employs the cofactor pyridoxal phosphate, also known as PLP, which participates in numerous enzymatic transamination, decarboxylation and deamination reactions.
In enzymology, a N-acetyldiaminopimelate deacetylase (EC 3.5.1.47) is an enzyme that catalyzes the chemical reaction
In enzymology, a succinyl-diaminopimelate desuccinylase (EC 3.5.1.18) is an enzyme that catalyzes the chemical reaction
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In enzymology, a N6-acetyl-beta-lysine transaminase is an enzyme that catalyzes the chemical reaction
In enzymology, an ornithine(lysine) transaminase (EC 2.6.1.68) is an enzyme that catalyzes the chemical reaction
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