3.4.19.1: acylaminoacyl-peptidase
This is an abbreviated version!
For detailed information about acylaminoacyl-peptidase, go to the full flat file.
Word Map on EC 3.4.19.1
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3.4.19.1
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marrow
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immunocytochemical
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oligopeptidase
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anti-alkaline
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prolyl
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immunophenotyping
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hla-dr
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smear
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cryosta
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phosphatase-anti-alkaline
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cytospins
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immunoenzymatic
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moabs
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aeropyrum
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pernix
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fluorophosphate
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immunoenzyme
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immunoalkaline
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medicine
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acylase
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cytocentrifuge
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analysis
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drug development
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synthesis
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degradation
- 3.4.19.1
- marrow
-
immunocytochemical
-
oligopeptidase
-
anti-alkaline
-
prolyl
-
immunophenotyping
-
hla-dr
-
smear
-
cryosta
-
phosphatase-anti-alkaline
-
cytospins
-
immunoenzymatic
-
moabs
-
aeropyrum
- pernix
- fluorophosphate
-
immunoenzyme
-
immunoalkaline
- medicine
- acylase
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cytocentrifuge
- analysis
- drug development
- synthesis
- degradation
Reaction
cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide =
Synonyms
AAP, AARE, AARE/OPH, AAREP, AcpH, acyl aminoacyl peptidase, acyl peptide hydrolase, Acyl-peptide hydrolase, acyl-peptide releasing enzyme, acylamino acid-releasing enzyme, acylamino acid-releasing enzyme/oxidized protein hydrolase, acylamino-acid-releasing enzyme, acylaminoacyl peptidase, Acylaminoacyl-peptidase, acylpeptide hydrolase, acylpeptide hydrolase/esterase, alpha-N-acylpeptide hydrolase, ApAAP, apAPH, APEH, APEH-1, apeH-2, APEH-3, APEH-3Ss, APEHs, APE_1547.1, APH, APHdr, AtAARE, BmAPH, cAARE, DNF15S2 protein, N-acylaminoacyl-peptide hydrolase, N-acylpeptide hydrolase, N-formylmethionine (fMet) aminopeptidase, OP85, PhAAP, pi-APH, PM hydrolase, PMH, SpAAP, sso2141, SSO2693, ST0779, yuxL
ECTree
3.4.19.1 acylaminoacyl-peptidaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.4.19.1 - acylaminoacyl-peptidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D524A
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
D524N
the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
F488G/R526V/T560W
1.55fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
H367A
displays significantly reduced catalytic activity. Unlike the reaction of the wild-type, the reaction of the mutant displays completely linear temperature dependence. Its reaction is associated with unfavourable entropy of activation
R526 I
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 17.3fold higher than the wild-type ratio
R526A
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 11.7fold higher than the wild-type ratio
R526E
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 115.5fold higher than the wild-type ratio
R526K
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 13.9fold higher than the wild-type ratio
R526L
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 14.8fold higher than the wild-type ratio
R526V
R526V/T560W
1.5fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V
W474V/F488G/R526V/T560W
the mutant enzyme has 7fold higher catalytic efficiency (kcat/Km) for 4-nitrophenyl dodecanoate than the mutant enzyme R526V
W474V/R526V/T560W
3.11fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
D524A
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the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
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D524N
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the mutation affects the closed, active form of the enzyme, disrupting its catalytic triad. The wild-type enzyme exhibits a bell-shaped pH-rate profile (optimum at pH 7.5), whereas the rate constants for the D524A and D524N variants increase to about pH 9. The kcat/Km values is much lower compared with those of the wild-type enzyme
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F488G/R526V/T560W
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1.55fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
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R526V
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mutant enzyme with high esterase activity, extreme thermal stability, and high tolerance to organic solvents
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R526V/T560W
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1.5fold increase in activity with 4-nitrophenyl dodecanoate compared to activity of mutant R526V
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W474V/R526V/T560W
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3.11fold increase in activity with 4-nitrophenyl laurate compared to activity of mutant R526V/T560W
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D15A
mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH
D15A/R18A
mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH
DELTA1-21
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optimal temperature of a truncated mutant of apAPH that lacks the first short alpha-helix at the N-terminal is decreased by 15°C
DELTAN21
mutant, N-terminal helix deleted, no longer functional at the optimum temperature, 95°C, for the wild-type enzyme, low thermodynamic stability
E88A
mutant, lower thermodynamic stability than the wild-type, broken inter-domain salt bridge, catalytic activity almost abolished
E88A/R526E
mutant, lower thermodynamic stability than the wild-type
E88A/R526K
mutant, lower thermodynamic stability than the wild-type, broken inter-domain salt bridge, positive charge at position 526, catalytic activity almost abolished
E88A/R526V
mutant, lower thermodynamic stability than the wild-type
R18A
mutant to determine the effects of the N-terminal region and the salt bridges on the stability and catalytic activity of apAPH
S445A
nearly inactive. Remaining activity of the mutant can cause cleavage in the peptide
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
E10A
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a 20-min pre-incubation at 50°C leads to a residual of 65% (wild-type: 70%)
K6A
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a 20-min pre-incubation at 50°C leads to a residual of 70% similar to wild-type
K6A/E10A
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a 20-min pre-incubation at 50°C leads to a residual of 45% (wild-type: 70%)
N3A
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a 20-min pre-incubation at 50°C leads to a residual of 70% similar to wild-type
R14A
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a 20-min pre-incubation at 50°C leads to a residual of 70% similar to wild-type
additional information
R526V
the ratio of kcat/Km for p-nitrophenyl caprylate to kcat/KM for N-acetyl-Leu-p-nitroanilide is 22.3fold higher than the wild-type ratio
R526V
mutant enzyme with high esterase activity, extreme thermal stability, and high tolerance to organic solvents
additional information
construction of chimeras of a carboxylesterase (EC 3.1.1.1) from Archaeoglobus fulgidus and an acylpeptide hydrolase (EC 3.4.19.1) from Aeropyrum pernix K1. Their activities to hydrolyze 4-nitrophenyl esters (pNP) with different acyl chain lengths is explored. The chimeras inherit the thermophilic property of both parents. The substrate-binding domain is the dominant factor on enzyme substrate specificity, and the optimization of the newly formed domain interface is an important guarantee for successful domain swapping of proteins with low-sequence homology
additional information
the esterase activity of the mutant R526V (this mutation transforms a promiscuous acylaminoacyl peptidase into a specific carboxylesterase) towards substrates with long acyl chains is enhanced by protein engineering and solvent optimization. The substrate preference of the enzyme can be further changed from 4-nitrophenyl octanoate to 4-nitrophenyl dodecanoate by protein and solvent engineering
additional information
construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
additional information
Aeropyrum pernix ATCC 700893
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construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
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additional information
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the esterase activity of the mutant R526V (this mutation transforms a promiscuous acylaminoacyl peptidase into a specific carboxylesterase) towards substrates with long acyl chains is enhanced by protein engineering and solvent optimization. The substrate preference of the enzyme can be further changed from 4-nitrophenyl octanoate to 4-nitrophenyl dodecanoate by protein and solvent engineering
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additional information
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construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
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additional information
Aeropyrum pernix JCM 9820
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construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
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additional information
Aeropyrum pernix NBRC 100138
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construction of mutant APE-DELTAEG by deletion of two residues E316 and G317, and of mutant APE-2G by inserted two Gly residues between residues L315 and E316 deleted residues F395 and V396. The catalytic activity of the APE-DELTAEG mutant toward 4-nitrophenyl butyrate (pNPC4) is 2.8fold more active compared to wild-type, whose preferred substrate is 4-nitrophenyl caprylate (pNPC8)
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additional information
enzyme mutants lacking the arm in the quarternary structure are monomeric, inactive and highly prone to aggregation
additional information
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enzyme mutants lacking the arm in the quarternary structure are monomeric, inactive and highly prone to aggregation
additional information
construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
additional information
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construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
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additional information
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construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
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additional information
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construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
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additional information
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construction of N-terminus deletion mutants DELTAN21 and DELTAN21-4 A, which can be obviously discriminated from the wild-type in terms of activity in various pH values. Mutant ST-4 A exhibits higher activity toward substrate Ac-Ala-Ala-Ala at 70°C compared with the wild-type enzyme. ST-4 A enzymatic activity is 2fold more active than wild-type at 95°C and ST-6 A enzymatic activity is 1.7fold more active than wild-type at 95°C. Construction of mutants ST-DELTAGL by deletion of residues G332 and L333, of mutant ST-2 A by insertion of four Ala residues between residues G331 and G332, of mutant ST-6 A by removal of N-terminal 21 residues and linker insertion with four Ala residues between residues G331 and G332, and of mutant DELTAN21, overview
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