EC Number   |
General Information |
Reference |
|---|
    3.5.1.54 | evolution |
allophanate hydrolase (AH) is a member of the AS family |
-, 753254 |
| 3.5.1.54 | evolution |
allophanate hydrolase is a member of the amidase family of enzymes that possess a conserved serine- and glycine-rich motif, the so-called amidase signature sequence |
733034 |
| 3.5.1.54 | evolution |
the enzyme belongs to the amidase signature family, which is characterized by a conserved block of 130 amino acids rich in Gly and Ser and a Ser-cisSer-Lys catalytic triad |
-, 733342 |
| 3.5.1.54 | evolution |
the positions of the amino acids essential for catalysis (Ser165, Ser189, and Lys91) and substrate binding (Tyr320 and Arg328), are highly conserved |
733179 |
| 3.5.1.54 | evolution |
urea carboxylase (UC) and allophanate hydrolase (A) display a close evolutionary and functional association. The inter-domain coupling efficiency is low in both bacterial and yeast UAL |
-, 746393 |
| 3.5.1.54 | malfunction |
the addition of inactive PsAHS179A reduces the overall catalytic activity by competitively binding to PsUC |
-, 746393 |
| 3.5.1.54 | metabolism |
allophanate hydrolase also participates in the cyanuric acid mineralization pathway, in which the cyanuric acid ring is hydrolytically opened by cyanuric acid hydrolase (AtzD or TrzD, EC 3.5.2.15) forming the unstable metabolite carboxybiuret, which spontaneously decarboxylates to form biuret. Allophanate is produced from biuret by AtzE (biuret hydrolase; EC 3.5.1.84) via a single deamination. Hydrolysis of allophanate is then carried out by allophanate hydrolase. Both pathways, cyanuric acid mineralization pathway and urea carboxylase pathway, depend upon allophanate deamination by allophanate hydrolase to avoid spontaneous decarboxylation (and urea formation) |
733034 |
| 3.5.1.54 | metabolism |
allophanate hydrolase catalyzes the hydrolysis of allophanate, an intermediate in atrazine degradation and urea catabolism pathways, to NH3 and CO2 |
-, 733342 |
| 3.5.1.54 | metabolism |
urea amidolyase catalyzes the conversion of urea to ammonium, the essential first step in utilizing urea as a nitrogen source |
-, 753037 |
| 3.5.1.54 | more |
binding process of allophanate to allophanate hydrolase, computational analysis using the three-dimensional structure of AH, PDB ID 4GYS, quantum chemistry calculations and molecular dynamics simulation, overview. The optimal enzyme-substrate complex conformation demonstrates that along with Arg307 and Tyr299, Gly124 is also one of the key anchor residues in the stable complex. The energetic calculation suggests the existence of an intermediate state in the enzyme-substrate binding process. The further atomic-level investigation illuminates that Tyr299, Arg307 and Ser172 can stabilize the substrate in the intermediate state. By this token, the residues Arg307 and Tyr299 function in both binding process and getting stable state. Active site structure with docked allophanate, overview |
-, 753254 |
