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Literature summary extracted from

  • Zhu, J.; Wang, Y.; Li, X.; Han, W.; Zhao, L.
    Understanding the interactions of different substrates with wild-type and mutant acylaminoacyl peptidase using molecular dynamics simulations (2018), J. Biomol. Struct. Dyn., 36, 4285-4302 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.4.19.1 R526V Ac-Leu-4-nitroanilide bound to R526V AAP to form a more disordered loop (residues 552-562) in the alpha/beta-hydrolase fold like of AAP, which causes an open and inactive AAP domain form, secondly, binding 4-nitrophenylcaprylate and Ac-Leu-4-nitroanilide to AAP can decrease the flexibility of residues 225-250, 260-270 and 425-450, in which the ordered secondary structures may contain the suitable geometrical structure and so it is useful to serine attack Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.4.19.1 Aeropyrum pernix Q9YBQ2
-
-
3.4.19.1 Aeropyrum pernix ATCC 700893 Q9YBQ2
-
-
3.4.19.1 Aeropyrum pernix DSM 11879 Q9YBQ2
-
-
3.4.19.1 Aeropyrum pernix JCM 9820 Q9YBQ2
-
-
3.4.19.1 Aeropyrum pernix NBRC 100138 Q9YBQ2
-
-
3.4.19.1 Homo sapiens P13798
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.1 4-nitrophenyl caprylate + H2O
-
 Aeropyrum pernix 4-nitrophenol + caprylate
-
 ?
3.4.19.1 4-nitrophenyl caprylate + H2O
-
 Homo sapiens 4-nitrophenol + caprylate
-
 ?
3.4.19.1 4-nitrophenyl caprylate + H2O
-
 Aeropyrum pernix ATCC 700893 4-nitrophenol + caprylate
-
 ?
3.4.19.1 4-nitrophenyl caprylate + H2O
-
 Aeropyrum pernix DSM 11879 4-nitrophenol + caprylate
-
 ?
3.4.19.1 4-nitrophenyl caprylate + H2O
-
 Aeropyrum pernix JCM 9820 4-nitrophenol + caprylate
-
 ?
3.4.19.1 4-nitrophenyl caprylate + H2O
-
 Aeropyrum pernix NBRC 100138 4-nitrophenol + caprylate
-
 ?
3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O
-
 Aeropyrum pernix N-acetyl-L-Leu + 4-nitroaniline
-
 ?
3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O
-
 Homo sapiens N-acetyl-L-Leu + 4-nitroaniline
-
 ?
3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O
-
 Aeropyrum pernix ATCC 700893 N-acetyl-L-Leu + 4-nitroaniline
-
 ?
3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O
-
 Aeropyrum pernix DSM 11879 N-acetyl-L-Leu + 4-nitroaniline
-
 ?
3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O
-
 Aeropyrum pernix JCM 9820 N-acetyl-L-Leu + 4-nitroaniline
-
 ?
3.4.19.1 N-acetyl-L-Leu-4-nitroanilide + H2O
-
 Aeropyrum pernix NBRC 100138 N-acetyl-L-Leu + 4-nitroaniline
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.19.1 AAP
-
 Aeropyrum pernix
3.4.19.1 AAP
-
 Homo sapiens
3.4.19.1 acylaminoacyl peptidase
-
 Aeropyrum pernix
3.4.19.1 acylaminoacyl peptidase
-
 Homo sapiens
3.4.19.1 ApAAP
-
 Aeropyrum pernix

General Information

EC Number General Information Comment Organism
3.4.19.1 evolution enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily Aeropyrum pernix
3.4.19.1 evolution enzyme AAP belongs to alpha/beta-hydrolase enzyme superfamily Homo sapiens
3.4.19.1 additional information substrate binding structures of wild-type and mutant enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations Aeropyrum pernix
3.4.19.1 additional information substrate binding structures of wild-type and mutant R526V enzymes, docking study and molecular dynamics simulations, overview. Molecular mechanics/Poisson-Boltzmann surface area (MM/PBSA) calculations Homo sapiens