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Literature summary extracted from

  • Nyyssoelae, A.; Pihlajaniemi, V.; Haekkinen, M.; Kontkanen, H.; Saloheimo, M.; Nakari-Setaelae, T.
    Cloning and characterization of a novel acidic cutinase from Sirococcus conigenus (2014), Appl. Microbiol. Biotechnol., 98, 3639-3650.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.74 gene ScCut1, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant of C-terminally His-tagged codon-optimized enzyme expression in Pichia pastoris strain X-33, subcloning in Escherichia coli Sirococcus conigenus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.74 additional information generation of codon-optimized enzyme for expression in Pichia pastoris Sirococcus conigenus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.74 1.67
-
 4-nitrophenyl butyrate pH 4.5, 25°C, recombinant enzyme Sirococcus conigenus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.74 extracellular
-
 Sirococcus conigenus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.74 additional information incubating the enzyme with 5 mM CaCl2, CoCl2, CuSO4, EDTA, FeCl2, MgCl2, MnCl2, Ni(NO3)2, ZnCl2, or 10 mM dithiothreitol has no significant effect on the 4-nitrophenyl butyrate hydrolysis activity Sirococcus conigenus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.1.74 cutin + H2O Sirococcus conigenus
-
 cutin monomers
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.74 Sirococcus conigenus S4VCH4 gene ScCut1
-
3.1.1.74 Sirococcus conigenus VTT D-04989 S4VCH4 gene ScCut1
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.74 no glycoprotein the enzyme contains no N- or O-glycosylation sites Sirococcus conigenus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.74 recombinant C-terminally His-tagged enzyme from Pichia pastoris by nickel affinity chromatography Sirococcus conigenus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.74 4-nitrophenyl acetate + H2O high activity Sirococcus conigenus 4-nitrophenol + acetate
-
 ?
3.1.1.74 4-nitrophenyl acetate + H2O high activity Sirococcus conigenus VTT D-04989 4-nitrophenol + acetate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Sirococcus conigenus 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl butyrate + H2O
-
 Sirococcus conigenus VTT D-04989 4-nitrophenol + butyrate
-
 ?
3.1.1.74 4-nitrophenyl hexanoate + H2O
-
 Sirococcus conigenus 4-nitrophenol + hexanoate
-
 ?
3.1.1.74 4-nitrophenyl hexanoate + H2O
-
 Sirococcus conigenus VTT D-04989 4-nitrophenol + hexanoate
-
 ?
3.1.1.74 4-nitrophenyl propionate + H2O high activity Sirococcus conigenus 4-nitrophenol + propionate
-
 ?
3.1.1.74 4-nitrophenyl propionate + H2O high activity Sirococcus conigenus VTT D-04989 4-nitrophenol + propionate
-
 ?
3.1.1.74 4-nitrophenyl valerate + H2O
-
 Sirococcus conigenus 4-nitrophenol + valerate
-
 ?
3.1.1.74 birch bark suberin + H2O
-
 Sirococcus conigenus ?
-
 ?
3.1.1.74 cutin + H2O
-
 Sirococcus conigenus cutin monomers
-
 ?
3.1.1.74 additional information the enzyme prefers shorter (C2 to C3) fatty acid esters of 4-nitrophenol to longer ones, no or poor activity with 4-nitrophenyl esters substrates of C10-C18, overview. The enzyme also shows lipase activity with olive oil as substrate Sirococcus conigenus ?
-
 ?
3.1.1.74 additional information the enzyme prefers shorter (C2 to C3) fatty acid esters of 4-nitrophenol to longer ones, no or poor activity with 4-nitrophenyl esters substrates of C10-C18, overview. The enzyme also shows lipase activity with olive oil as substrate Sirococcus conigenus VTT D-04989 ?
-
 ?
3.1.1.74 tritiated apple cutin + H2O
-
 Sirococcus conigenus ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.74 acidic cutinase
-
 Sirococcus conigenus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.74 25
-
 assay at, 4-nitrophenyl ester substrates Sirococcus conigenus
3.1.1.74 40
-
 assay at, tritiated cutin substrate Sirococcus conigenus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.74 4 25 purified recombinant enzyme, pH 4.5, completely stable at Sirococcus conigenus
3.1.1.74 42
-
 purified recombinant enzyme, pH 4.5, half-life is 46-76 h Sirococcus conigenus
3.1.1.74 55
-
 purified recombinant enzyme, pH 4.5, half-life is 40 min Sirococcus conigenus
3.1.1.74 65
-
 purified recombinant enzyme, pH 4.5, half-life is 30 min Sirococcus conigenus
3.1.1.74 80
-
 denaturation of recombinant enzyme by heating the protein sample to 80 °C is to a great extent reversible Sirococcus conigenus
3.1.1.74 85
-
 purified recombinant enzyme, pH 4.5, half-life is 24 min Sirococcus conigenus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.74 4.1 4.6 substrate tritiated cutin, recombinant enzyme Sirococcus conigenus
3.1.1.74 4.7 5.2 substrate 4-nitrophenyl butyrate, recombinant enzyme Sirococcus conigenus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.74 3 7.5 the enzyme is active over a broad pH range, 25% of maximal activity at pH 3.0 Sirococcus conigenus

General Information

EC Number General Information Comment Organism
3.1.1.74 evolution the enzyme contains the conserved motif G-Y-S-Q-G surrounding the active site serine as well as the aspartic acid and histidine residues of the cutinase active site Sirococcus conigenus