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Literature summary extracted from

  • Liu, D.; Deng, L.; Wang, D.; Li, W.; Gao, R.
    "Bridge regions" regulate catalysis and protein stability of acylpeptide hydrolase (2019), Biochem. Eng. J., 145, 42-52 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.19.1 gene APE_1547.1, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Aeropyrum pernix
3.4.19.1 gene ST0779, sequence comparisons, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3) Sulfurisphaera tokodaii

Protein Variants

EC Number Protein Variants Comment Organism
3.4.19.1 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) Aeropyrum pernix
3.4.19.1 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 Sulfurisphaera tokodaii

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 Sulfurisphaera tokodaii Q973W9 i.e. Sulfolobus tokodaii
-
3.4.19.1 Sulfurisphaera tokodaii 7 Q973W9 i.e. Sulfolobus tokodaii
-
3.4.19.1 Sulfurisphaera tokodaii DSM 16993 Q973W9 i.e. Sulfolobus tokodaii
-
3.4.19.1 Sulfurisphaera tokodaii JCM 10545 Q973W9 i.e. Sulfolobus tokodaii
-
3.4.19.1 Sulfurisphaera tokodaii NBRC 100140 Q973W9 i.e. Sulfolobus tokodaii
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.19.1 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Aeropyrum pernix
3.4.19.1 recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Sulfurisphaera tokodaii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.19.1 Ac-Ala-Ala + H2O
-
Aeropyrum pernix Ac-Ala + Ala
-
?
3.4.19.1 Ac-Ala-Ala + H2O
-
Sulfurisphaera tokodaii Ac-Ala + Ala
-
?
3.4.19.1 Ac-Ala-Ala + H2O
-
Aeropyrum pernix ATCC 700893 Ac-Ala + Ala
-
?
3.4.19.1 Ac-Ala-Ala + H2O
-
Aeropyrum pernix DSM 11879 Ac-Ala + Ala
-
?
3.4.19.1 Ac-Ala-Ala + H2O
-
Aeropyrum pernix JCM 9820 Ac-Ala + Ala
-
?
3.4.19.1 Ac-Ala-Ala + H2O
-
Sulfurisphaera tokodaii 7 Ac-Ala + Ala
-
?
3.4.19.1 Ac-Ala-Ala + H2O
-
Sulfurisphaera tokodaii DSM 16993 Ac-Ala + Ala
-
?
3.4.19.1 Ac-Ala-Ala + H2O
-
Sulfurisphaera tokodaii JCM 10545 Ac-Ala + Ala
-
?
3.4.19.1 Ac-Ala-Ala + H2O
-
Aeropyrum pernix NBRC 100138 Ac-Ala + Ala
-
?
3.4.19.1 Ac-Ala-Ala + H2O
-
Sulfurisphaera tokodaii NBRC 100140 Ac-Ala + Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala + H2O
-
Aeropyrum pernix Ac-Ala + Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii Ac-Ala + Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala + H2O
-
Aeropyrum pernix ATCC 700893 Ac-Ala + Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala + H2O
-
Aeropyrum pernix DSM 11879 Ac-Ala + Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala + H2O
-
Aeropyrum pernix JCM 9820 Ac-Ala + Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii 7 Ac-Ala + Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii DSM 16993 Ac-Ala + Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii JCM 10545 Ac-Ala + Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala + H2O
-
Aeropyrum pernix NBRC 100138 Ac-Ala + Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii NBRC 100140 Ac-Ala + Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O
-
Aeropyrum pernix Ac-Ala + Ala-Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O
-
Sulfurisphaera tokodaii Ac-Ala + Ala-Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O
-
Aeropyrum pernix ATCC 700893 Ac-Ala + Ala-Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O
-
Aeropyrum pernix DSM 11879 Ac-Ala + Ala-Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O
-
Aeropyrum pernix JCM 9820 Ac-Ala + Ala-Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O
-
Sulfurisphaera tokodaii 7 Ac-Ala + Ala-Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O
-
Sulfurisphaera tokodaii DSM 16993 Ac-Ala + Ala-Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O
-
Sulfurisphaera tokodaii JCM 10545 Ac-Ala + Ala-Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O
-
Aeropyrum pernix NBRC 100138 Ac-Ala + Ala-Ala-Ala
-
?
3.4.19.1 Ac-Ala-Ala-Ala-Ala + H2O
-
Sulfurisphaera tokodaii NBRC 100140 Ac-Ala + Ala-Ala-Ala
-
?
3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview Aeropyrum pernix ?
-
?
3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition Sulfurisphaera tokodaii ?
-
?
3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview Aeropyrum pernix ATCC 700893 ?
-
?
3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview Aeropyrum pernix DSM 11879 ?
-
?
3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview Aeropyrum pernix JCM 9820 ?
-
?
3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition Sulfurisphaera tokodaii 7 ?
-
?
3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition Sulfurisphaera tokodaii DSM 16993 ?
-
?
3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition Sulfurisphaera tokodaii JCM 10545 ?
-
?
3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview Aeropyrum pernix NBRC 100138 ?
-
?
3.4.19.1 additional information the acylpeptide hydrolase and esterase activity of wild-type and the mutants is tested with acetyl-amino acid-4-nitroanilides (Ac-Ala2, Ac-Ala3, Ac-Ala4) as the APH substrate and 4-nitrophenyl fatty acid esters (pNPC2, pNPC3, pNPC4, pNPC8, pNPC12, pNPC16) as esterase substrate. Substrate specificity of wild-type and mutant enzymes, overview. Promiscuous activity of the ST0779 mutant in aldol addition Sulfurisphaera tokodaii NBRC 100140 ?
-
?

Subunits

EC Number Subunits Comment Organism
3.4.19.1 More APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility Aeropyrum pernix
3.4.19.1 More APH family is composed of a beta-propeller domain in N-terminus and a catalytic domain in C-terminus. These domains are structurally connected by bridge regions. One is the N-terminus region that stretches into the C-terminal catalytic domain. The other is the linker that directly connects the beta-propeller domain to the catalytic domain. N-terminus region forms a unique alpha-helix 1 (alpha1), which deviates from the beta-propeller domain. Nevertheless, it connects with the surface of the catalytic domain. The structure of alpha1 is conserved and affects conformational flexibility Sulfurisphaera tokodaii

Synonyms

EC Number Synonyms Comment Organism
3.4.19.1 acylpeptide hydrolase
-
Aeropyrum pernix
3.4.19.1 acylpeptide hydrolase
-
Sulfurisphaera tokodaii
3.4.19.1 APE_1547.1
-
Aeropyrum pernix
3.4.19.1 APH
-
Aeropyrum pernix
3.4.19.1 APH
-
Sulfurisphaera tokodaii
3.4.19.1 ST0779
-
Sulfurisphaera tokodaii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.19.1 70
-
recombinant wild-type enzyme Sulfurisphaera tokodaii
3.4.19.1 95
-
recombinant mutant enzymes Sulfurisphaera tokodaii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.19.1 additional information
-
the enzyme is thermophilic Aeropyrum pernix
3.4.19.1 additional information
-
the enzyme is thermophilic Sulfurisphaera tokodaii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.19.1 8
-
recombinant wild-type and mutant enzymes Sulfurisphaera tokodaii

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.4.19.1 5 10 inactivation of wild-type enzyme at pH 10.0 Sulfurisphaera tokodaii
3.4.19.1 5 9.5 inactivation of enzyme mutants at pH 9.0-9.5 Sulfurisphaera tokodaii

General Information

EC Number General Information Comment Organism
3.4.19.1 additional information enzyme structure modeling and comparison with the enzyme structure from Aeropyrum pernix, overview. Both enzymes share a high structural homology Sulfurisphaera tokodaii
3.4.19.1 additional information enzyme structure modeling and comparison with the enzyme structure from Sulfurisphaera tokodaii, overview. Both enzymes share a high structural homology Aeropyrum pernix