EC Number   |
General Information |
Reference |
|---|
   5.4.3.11 | evolution |
phenylalanine 2,3-mutases, PAMs, belong to the class I lyase-like family that includes tyrosine 2,3-aminomutases (TAMs), tyrosine ammonia-lyases (TALs), and histidine ammonia-lyases (HALs). All these enzymes rely on a protein-derived cofactor, 4-methylideneimidazol-5-one (MIO), which is generated autocatalytically from three active site residues, Ala-Ser-Gly (Thr-Ser-Gly in PaPAM), forming a MIO signature motif |
749387 |
| 5.4.3.11 | evolution |
the enzyme belongs to a class I lyase-like superfamily of catalysts, along with other MIO-dependent aminomutases |
746575 |
| 5.4.3.11 | malfunction |
a hitA knockout mutant shows no hitachimycin production, but antibiotic production is restored by feeding with (S)-beta-Phe |
-, 747538 |
| 5.4.3.11 | metabolism |
the enzyme is important in the hitachimycin biosynthetic pathway. A plausible biosynthetic pathway for hitachimycin, including a unique polyketide skeletal transformation mechanism, is proposed |
-, 747538 |
| 5.4.3.11 | more |
enzyme structure-activity analysis and modeling of substrate-PaPAM structural interactions, overview |
746575 |
| 5.4.3.11 | more |
molecular modelling of the covalent enzyme-substrate N-MIO complexes in PaPAM |
749290 |
| 5.4.3.11 | physiological function |
PaPAM makes the (3S)-beta-phenylalanine antipode on the biosynthetic pathway to the antibiotic andrimid starting from (S)-beta-phenylalanine via (S)-alpha-phenylalanine |
746575 |
