EC Number   |
General Information |
Reference |
|---|
  1.14.13.33 | evolution |
amino acid sequences of NADH-preferring PHBHs of putative PHBHs identified in currently available bacterial genomes, phylogenetic analysis, overview. The pyridine nucleotide coenzyme specificity of PHBH emerged through adaptive evolution, and the NADH-preferring enzymes are the older versions of PHBH. Structural comparison and distance tree analysis of group A flavoprotein monooxygenases indicates that a similar protein segment as being responsible for the pyridine nucleotide coenzyme specificity of PHBH is involved in determining the pyridine nucleotide coenzyme specificity of the other group A members. Evolutionary rate calculation. Among the actinobacterial sequences presently available, most comprise the NADH-preferring fingerprint. However, Mycobacteria have a mixed type motif, often the first or both arginine(s) of the NADH-fingerprint are present but the remaining part is lacking. In addition, many mycobacterial sequences have parts of the NADPH-preferring fingerprint, especially, x(D/E)YVL(G/S)R |
-, 764761 |
| 1.14.13.33 | metabolism |
the enzyme is involved in the degradation of 4-hydroxybenzoate. The 4-hydroxybenzoate degradation pathway is required for full pathogenicity of Xanthomonas campestris pv. campestris in radish |
743802 |
| 1.14.13.33 | more |
energy profiling from enzyme protein structure is realized by means of a coarse-grained residue-level pair potential function modeling, overview |
-, 764761 |
| 1.14.13.33 | more |
the X-ray crystal structure of PraI is solved and reveals absolute conservation of the active site architecture to other PHBH structures despite their differing cofactor preferences |
765326 |
| 1.14.13.33 | physiological function |
the transformation of 4-hydroxybenzoate (4-HBA) to protocatechuate (PCA) is catalyzed by flavoprotein oxygenases known as para-hydroxybenzoate-3-hydroxylases (PHBHs) |
765326 |
