| Primary Identifier | IPR005960 | Type | Family |
| Short Name | Phe-4-hydroxylase_mono |
| description | This entry represents the small, monomeric form of phenylalanine-4-hydroxylase (PAH; ), as found in a certain Gram-negative bacteria. The enzyme is biopterin and metal dependent, and acts to irreversibly convert phenylalanine to tyrosine, the rate-limiting step in phenylalanine catabolism in some systems:L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + dihydrobiopterin + H2O The structure of PAH from Colwellia psychrerythraea (strain 34H / ATCC BAA-681), which binds tetrahydrobiopterin (BH4) as cofactor, is a cold-active form of the enzyme that has increased stability and flexibility around the active site []. |
