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Literature summary for 3.1.1.74 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
Search for more literature for 3.1.1.74

Cloned(Commentary)

Cloned (Comment) Organism
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

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

KM Value [mM]

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

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Sirococcus conigenus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
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)

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

Organism

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

Posttranslational Modification

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

Purification (Commentary)

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl acetate + H2O high activity Sirococcus conigenus 4-nitrophenol + acetate
-
 ?
4-nitrophenyl acetate + H2O high activity Sirococcus conigenus VTT D-04989 4-nitrophenol + acetate
-
 ?
4-nitrophenyl butyrate + H2O
-
 Sirococcus conigenus 4-nitrophenol + butyrate
-
 ?
4-nitrophenyl butyrate + H2O
-
 Sirococcus conigenus VTT D-04989 4-nitrophenol + butyrate
-
 ?
4-nitrophenyl hexanoate + H2O
-
 Sirococcus conigenus 4-nitrophenol + hexanoate
-
 ?
4-nitrophenyl hexanoate + H2O
-
 Sirococcus conigenus VTT D-04989 4-nitrophenol + hexanoate
-
 ?
4-nitrophenyl propionate + H2O high activity Sirococcus conigenus 4-nitrophenol + propionate
-
 ?
4-nitrophenyl propionate + H2O high activity Sirococcus conigenus VTT D-04989 4-nitrophenol + propionate
-
 ?
4-nitrophenyl valerate + H2O
-
 Sirococcus conigenus 4-nitrophenol + valerate
-
 ?
birch bark suberin + H2O
-
 Sirococcus conigenus ?
-
 ?
cutin + H2O
-
 Sirococcus conigenus cutin monomers
-
 ?
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 ?
-
 ?
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 ?
-
 ?
tritiated apple cutin + H2O
-
 Sirococcus conigenus ?
-
 ?

Synonyms

Synonyms Comment Organism
acidic cutinase
-
 Sirococcus conigenus

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

pH Optimum

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

pH Range

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

General Information

General Information Comment Organism
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