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Literature summary for 3.4.19.1 extracted from

  • Jin, H.; Zhu, J.; Dong, Y.; Han, W.
    Exploring the different ligand escape pathways in acylaminoacyl peptidase by random acceleration and steered molecular dynamics simulations (2016), RSC Adv., 6, 10987-10996 .
No PubMed abstract available
Search for more literature for 3.4.19.1

Organism

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YBQ2
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Reaction

Reaction Comment Organism Reaction ID
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide substrate binding and catalytic mechanisms, overview. Three main pathways are observed most frequently, namely P1, P2A, and P3, evaluation by comparing the average force profiles and potential of mean force calculations revealing that P3 is the unbinding pathway. P1 is located in a tunnel in the beta-propeller domain and contained the D158, R160, S157, S201, A200, S199, W250, D69, Q28, and R287 residues. P2A is located between blades 1 and 2 (G86, E88, K85, H90, D82, and N65), whereas P2D penetrates through blades 1 and 2 formed by loop A, which is close to P2A (S481, F485, D482, L115, I114, R113, H90, E88, R526, and S525). P3 is located between the beta-propeller domain and alpha/beta hydrolase containing the residues M561, A564, L568, F381, T380, I20, A21, F41, K24, G40, G44, and V46 Aeropyrum pernix
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ac-Leu-4-nitroanilide + H2O
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 Aeropyrum pernix Ac-Leu + 4-nitroaniline
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additional information the enzyme is also active with fatty acid esters, e.g. with 4-nitrophenyl caprylate. Substrate binding mechanism analysis, and random acceleration and steered molecular dynamics simulations of ligands unbinding pathways from APH. Three main pathways are observed most frequently, namely P1, P2A, and P3, evaluation by comparing the average force profiles and potential of mean force calculations revealing that P3 is the unbinding pathway. Overview Aeropyrum pernix ?
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Synonyms

Synonyms Comment Organism
acylpeptide hydrolase
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 Aeropyrum pernix
APH
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 Aeropyrum pernix

General Information

General Information Comment Organism
evolution the enzyme belongs to a class of serine-type protease belonging to the prolyl oligopeptidase (POP) family. The members of the POP family are involved in numerous metabolic processes Aeropyrum pernix
additional information molecular docking and molecular dynamics simulations using the structure with PDB ID 1VE7, substrate binding structures, overview Aeropyrum pernix