Crystallization (Comment) | Organism |
---|---|
three-dimensional structure analysis using PDB ID 4GYS | Granulibacter bethesdensis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
urea-1-carboxylate + H2O | Granulibacter bethesdensis | - |
2 CO2 + 2 NH3 | - |
? | |
urea-1-carboxylate + H2O | Granulibacter bethesdensis ATCC BAA-1260 | - |
2 CO2 + 2 NH3 | - |
? | |
urea-1-carboxylate + H2O | Granulibacter bethesdensis CGDNIH1 | - |
2 CO2 + 2 NH3 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Granulibacter bethesdensis | Q0BRB0 | - |
- |
Granulibacter bethesdensis ATCC BAA-1260 | Q0BRB0 | - |
- |
Granulibacter bethesdensis CGDNIH1 | Q0BRB0 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | binding process of allophanate to allophanate hydrolase, computational analysis, enzyme-substrate interaction, overview | Granulibacter bethesdensis | ? | - |
? | |
additional information | binding process of allophanate to allophanate hydrolase, computational analysis, enzyme-substrate interaction, overview | Granulibacter bethesdensis ATCC BAA-1260 | ? | - |
? | |
additional information | binding process of allophanate to allophanate hydrolase, computational analysis, enzyme-substrate interaction, overview | Granulibacter bethesdensis CGDNIH1 | ? | - |
? | |
urea-1-carboxylate + H2O | - |
Granulibacter bethesdensis | 2 CO2 + 2 NH3 | - |
? | |
urea-1-carboxylate + H2O | - |
Granulibacter bethesdensis ATCC BAA-1260 | 2 CO2 + 2 NH3 | - |
? | |
urea-1-carboxylate + H2O | - |
Granulibacter bethesdensis CGDNIH1 | 2 CO2 + 2 NH3 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
GbCGDNIH1_1744 | - |
Granulibacter bethesdensis |
General Information | Comment | Organism |
---|---|---|
evolution | allophanate hydrolase (AH) is a member of the AS family | Granulibacter bethesdensis |
additional information | 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 | Granulibacter bethesdensis |
physiological function | allophanate hydrolase catalyzes the hydrolysis reaction of allophanate, an intermediate in Atrazine degradation and urea catabolism pathways, to produce ammonia and carbon dioxide | Granulibacter bethesdensis |