Description

IPR015421 is a Pyridoxal phosphate-dependent transferase, major domain.

<p>The monomer of PLP-dependent transferases consists of two domains, a large domain and a small domain. This entry represents the large domain, which has a 3-layer α/β/α sandwich topology [[cite:PUB00043268]]. This domain can be found in the following PLP-dependent transferase families:</p> <ul> <li>Aspartate aminotransferase (AAT)-like enzymes, such as aromatic aminoacid aminotransferase AroAT, glutamine aminotransferase and kynureninase [[cite:PUB00035511]].</li> <li>Beta-eliminating lyases, such as tyrosine phenol lyase and tryptophanase [[cite:PUB00035512]].</li> <li>Pyridoxal-dependent decarboxylases, such as DOPA decarboxylase and glutamate decarboxylase beta (GadB) [[cite:PUB00035513]].</li> <li>Cystathionine synthase-like enzymes, such as cystalysin, methionine gamma-lyase (MGL), and cysteine desulphurase (IscS) [[cite:PUB00035514]].</li> <li>GABA-aminotransferase-like enzymes, such as ornithine aminotransferase and serine hydroxymethyltransferase [[cite:PUB00035515]].</li> <li>Ornithine decarboxylase major domain [[cite:PUB00014087]].</li> </ul> <p>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:PUB00035505], [cite:PUB00006322], [cite:PUB00035506]]. 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 [[cite:PUB00035507]]. Inadequate levels of pyridoxal phosphate in the brain can cause neurological dysfunction, particularly epilepsy [[cite:PUB00035508]].</p> <p>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 [[cite:PUB00035504]].</p>

This description is obtained from EB-eye REST.

Associated GO terms

GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on April 27, 2020, while the GO metadata was last updated on April 27, 2020.

Associated Lotus transcripts 364