EC Number   |
General Information |
Reference |
|---|
    1.14.13.2 | 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 |
| 1.14.13.2 | evolution |
evolutionary relationship between the NAD(P)H-dependent FAD-containing 4-hydroxybenzoate hydroxylases and phylogenetic analysis of group A FPMOs, overview |
-, 764036 |
| 1.14.13.2 | evolution |
phylogenetic analysis shows that FAD-dependent 4-hydroxybenzoate hydroxylases reside in distinct clades of the group A flavoprotein monooxygenase (FPMO) family, indicating their separate divergence from a common ancestor. Protein homology modeling reveals that the fungal 4-hydroxybenzoate 3-hydroxylase PhhA is structurally related to phenol hydroxylase (PHHY) and 3-hydroxybenzoate 4-hydroxylase (3HB4H). 4-Hydroxybenzoate 1-hydroxylase (4HB1H) from yeast catalyzes an oxidative decarboxylation reaction and is structurally similar to 3-hydroxybenzoate 6-hydroxylase (3HB6H), salicylate hydroxylase (SALH) and 6-hydroxynicotinate 3-monooxygenase (6HNMO). Group A FPMOs are involved in the aerobic microbial catabolism of 4-hydroxybenzoate. Phylogenetic analysis and structure comparisons, detailed overview |
-, 764036 |
| 1.14.13.2 | evolution |
the PobA enzyme structure is highly conserved across various organisms. Active-site residues Tyr201, Ser212, Arg214, Tyr222 and Pro293 interact with the carboxyl and phenolic components of 4-HB and are essential for its oxidative catalysis |
-, 763846 |
| 1.14.13.2 | malfunction |
replacement of Tyr385 with Phe forms a mutant, which enables the production of 3,4,5-trihydroxybenzonate (gallic acid) from 3,4-DOHB, although the catalytic activity of the mutant is quite low. The L199V/Y385F double mutant exhibits activity for producing gallic acid 4.3fold higher than that of the Y385F single mutant. This improvement in catalytic activity is primarily due to the suppression of a shunt reaction that wasts NADPH by producing H2O2, molecular mechanism underlying this higher catalytic activity, molecular dynamics simulations and quantum mechanics/molecular mechanics calculations, overview |
-, 764168 |
| 1.14.13.2 | metabolism |
enzyme PHBH is almost exclusively found in prokaryotes, where its induction, usually as a consequence of lignin degradation, results in the regioselective formation of protocatechuate, one of the central intermediates in the global carbon cycle |
-, 764036 |
| 1.14.13.2 | metabolism |
the NADPH-dependent 4-HBA hydroxylase from Pseudomonas aeruginosa (Pa PobA) natively catalyzes the first step in gallic acid biosynthesis |
-, 763785 |
| 1.14.13.2 | more |
energy profiling from enzyme protein structure is realized by means of a coarse-grained residue-level pair potential function modeling, overview |
764761 |
| 1.14.13.2 | more |
enzyme protein homology modeling of An_PhhA using the structure file of Tc_PHHY (PDB ID 1pn0) as template, overview. Hydroxylase enzymes structure comparisons, overview |
-, 764036 |
| 1.14.13.2 | more |
in wild-type PobA structure (PDB ID 1IUW), the productive binding mode is described by the hydrogen-bonding networks stabilizing 4-HBA and positioning the 3-carbon toward FAD for hydroxylation, comparison with enzyme mutants Da015 and DA016 |
-, 763785 |
