Pyridoxal phosphate-dependent transferase, small domain
IPR015422
Definition
The monomer of PLP-dependent transferases consists of two domains, a large domain and a small domain. This entry represents small domain, which has a complex α/β structure PMID:17583737. It can be found in the following PLP-dependent transferase families: Aspartate aminotransferase (AAT)-like enzymes, such as aromatic aminoacid aminotransferase AroAT, glutamine aminotransferase and kynureninase PMID:17300176. Beta-eliminating lyases, such as tyrosine phenol lyase and tryptophanase PMID:16790938. Pyridoxal-dependent decarboxylases, such as DOPA decarboxylase and glutamate decarboxylase beta (GadB) PMID:15690345. Cystathionine synthase-like enzymes, such as cystalysin, methionine gamma-lyase (MGL), and cysteine desulphurase (IscS) PMID:17014820. GABA-aminotransferase-like enzymes, such as ornithine aminotransferase and serine hydroxymethyltransferase PMID:15848278. Ornithine decarboxylase PMID:10666573. CMP-5'-(3-aminopropyl)phosphonate synthase PMID:20142041. Canavanine gamma-lyase PMID:36320885. Pyridoxal phosphate is the active form of vitamin B6 (pyridoxine or pyridoxal). Pyridoxal 5'-phosphate (PLP) is a versatile catalyst, acting as a coenzyme in a multitude of reactions, including decarboxylation, deamination and transamination [[cite:PMID:8690703], [cite:PMID:7748903], [cite:PMID:15189147]]. PLP-dependent enzymes are primarily involved in the biosynthesis of amino acids and amino acid-derived metabolites, but they are also found in the biosynthetic pathways of amino sugars and in the synthesis or catabolism of neurotransmitters; pyridoxal phosphate can also inhibit DNA polymerases and several steroid receptors PMID:17109392. Inadequate levels of pyridoxal phosphate in the brain can cause neurological dysfunction, particularly epilepsy PMID:16763894. PLP enzymes exist in their resting state as a Schiff base, the aldehyde group of PLP forming a linkage with the ε-amino group of an active site lysine residue on the enzyme. The α-amino group of the substrate displaces the lysine ε-amino group, in the process forming a new aldimine with the substrate. This aldimine is the common central intermediate for all PLP-catalysed reactions, enzymatic and non-enzymatic PMID:15581583.
33 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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