1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR015421 | Domain | Pyridoxal phosphate-dependent transferase, major region, subdomain 1 |
| Type: | Family | Name: | Pyridoxal phosphate-dependent transferase, archaea |
| Description: | 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 [, , ]. 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 []. Inadequate levels of pyridoxal phosphate in the brain can cause neurological dysfunction, particularly epilepsy [].PLP enzymes exist in their resting state as a Schiff base, the aldehyde group of PLP forming a linkage with the epsilon-amino group of an active site lysine residue on the enzyme. The alpha-amino group of the substrate displaces the lysine epsilon-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 [].This entry represents pyridoxal phosphate enzymes of unknown function found in archaea. Sequence similarity to SelA, a bacterial enzyme of selenocysteine biosynthesis, has led to some members being misannotated as functionally equivalent, but selenocysteine is made on tRNA in Archaea by a two-step process that does not involve a SelA homolog. | Short Name: | PyrdxlP-dep_transferase_arc |
| DB identifier | Type | Name |
|---|---|---|
| IPR015421 | Domain | Pyridoxal phosphate-dependent transferase, major region, subdomain 1 |
