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Literature summary for 3.5.1.54 extracted from

  • Zhang, Z.; Zhang, J.; Zheng, Q.; Kong, C.; Li, Z.; Zhang, H.; Ma, J.
    Theoretical investigation on binding process of allophanate to allophanate hydrolase (2015), Chem. Res. Chin. Univ., 31, 1023-1028 .
No PubMed abstract available
Search for more literature for 3.5.1.54

Crystallization (Commentary)

Crystallization (Comment) Organism
three-dimensional structure analysis using PDB ID 4GYS Granulibacter bethesdensis

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Granulibacter bethesdensis Q0BRB0
-
-
Granulibacter bethesdensis ATCC BAA-1260 Q0BRB0
-
-
Granulibacter bethesdensis CGDNIH1 Q0BRB0
-
-

Substrates and Products (Substrate)

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

Synonyms Comment Organism
GbCGDNIH1_1744
-
 Granulibacter bethesdensis

General Information

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