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Literature summary for 3.4.19.1 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
Search for more literature for 3.4.19.1

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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

Organism UniProt Comment Textmining
Aeropyrum pernix Q9YBQ2
-
-
Aeropyrum pernix ATCC 700893 Q9YBQ2
-
-
Aeropyrum pernix DSM 11879 Q9YBQ2
-
-
Aeropyrum pernix JCM 9820 Q9YBQ2
-
-
Aeropyrum pernix NBRC 100138 Q9YBQ2
-
-
Sulfurisphaera tokodaii Q973W9 i.e. Sulfolobus tokodaii
-
Sulfurisphaera tokodaii 7 Q973W9 i.e. Sulfolobus tokodaii
-
Sulfurisphaera tokodaii DSM 16993 Q973W9 i.e. Sulfolobus tokodaii
-
Sulfurisphaera tokodaii JCM 10545 Q973W9 i.e. Sulfolobus tokodaii
-
Sulfurisphaera tokodaii NBRC 100140 Q973W9 i.e. Sulfolobus tokodaii
-

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ac-Ala-Ala + H2O
-
 Aeropyrum pernix Ac-Ala + Ala
-
 ?
Ac-Ala-Ala + H2O
-
 Sulfurisphaera tokodaii Ac-Ala + Ala
-
 ?
Ac-Ala-Ala + H2O
-
 Aeropyrum pernix ATCC 700893 Ac-Ala + Ala
-
 ?
Ac-Ala-Ala + H2O
-
 Aeropyrum pernix DSM 11879 Ac-Ala + Ala
-
 ?
Ac-Ala-Ala + H2O
-
 Aeropyrum pernix JCM 9820 Ac-Ala + Ala
-
 ?
Ac-Ala-Ala + H2O
-
 Sulfurisphaera tokodaii 7 Ac-Ala + Ala
-
 ?
Ac-Ala-Ala + H2O
-
 Sulfurisphaera tokodaii DSM 16993 Ac-Ala + Ala
-
 ?
Ac-Ala-Ala + H2O
-
 Sulfurisphaera tokodaii JCM 10545 Ac-Ala + Ala
-
 ?
Ac-Ala-Ala + H2O
-
 Aeropyrum pernix NBRC 100138 Ac-Ala + Ala
-
 ?
Ac-Ala-Ala + H2O
-
 Sulfurisphaera tokodaii NBRC 100140 Ac-Ala + Ala
-
 ?
Ac-Ala-Ala-Ala + H2O
-
 Aeropyrum pernix Ac-Ala + Ala-Ala
-
 ?
Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii Ac-Ala + Ala-Ala
-
 ?
Ac-Ala-Ala-Ala + H2O
-
 Aeropyrum pernix ATCC 700893 Ac-Ala + Ala-Ala
-
 ?
Ac-Ala-Ala-Ala + H2O
-
 Aeropyrum pernix DSM 11879 Ac-Ala + Ala-Ala
-
 ?
Ac-Ala-Ala-Ala + H2O
-
 Aeropyrum pernix JCM 9820 Ac-Ala + Ala-Ala
-
 ?
Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii 7 Ac-Ala + Ala-Ala
-
 ?
Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii DSM 16993 Ac-Ala + Ala-Ala
-
 ?
Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii JCM 10545 Ac-Ala + Ala-Ala
-
 ?
Ac-Ala-Ala-Ala + H2O
-
 Aeropyrum pernix NBRC 100138 Ac-Ala + Ala-Ala
-
 ?
Ac-Ala-Ala-Ala + H2O high activity Sulfurisphaera tokodaii NBRC 100140 Ac-Ala + Ala-Ala
-
 ?
Ac-Ala-Ala-Ala-Ala + H2O
-
 Aeropyrum pernix Ac-Ala + Ala-Ala-Ala
-
 ?
Ac-Ala-Ala-Ala-Ala + H2O
-
 Sulfurisphaera tokodaii Ac-Ala + Ala-Ala-Ala
-
 ?
Ac-Ala-Ala-Ala-Ala + H2O
-
 Aeropyrum pernix ATCC 700893 Ac-Ala + Ala-Ala-Ala
-
 ?
Ac-Ala-Ala-Ala-Ala + H2O
-
 Aeropyrum pernix DSM 11879 Ac-Ala + Ala-Ala-Ala
-
 ?
Ac-Ala-Ala-Ala-Ala + H2O
-
 Aeropyrum pernix JCM 9820 Ac-Ala + Ala-Ala-Ala
-
 ?
Ac-Ala-Ala-Ala-Ala + H2O
-
 Sulfurisphaera tokodaii 7 Ac-Ala + Ala-Ala-Ala
-
 ?
Ac-Ala-Ala-Ala-Ala + H2O
-
 Sulfurisphaera tokodaii DSM 16993 Ac-Ala + Ala-Ala-Ala
-
 ?
Ac-Ala-Ala-Ala-Ala + H2O
-
 Sulfurisphaera tokodaii JCM 10545 Ac-Ala + Ala-Ala-Ala
-
 ?
Ac-Ala-Ala-Ala-Ala + H2O
-
 Aeropyrum pernix NBRC 100138 Ac-Ala + Ala-Ala-Ala
-
 ?
Ac-Ala-Ala-Ala-Ala + H2O
-
 Sulfurisphaera tokodaii NBRC 100140 Ac-Ala + Ala-Ala-Ala
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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 ?
-
 ?
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

Subunits Comment Organism
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
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

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

pH Optimum

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

pH Range

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

General Information

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