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Literature summary for 3.1.1.74 extracted from

  • Shirke, A.N.; Basore, D.; Holton, S.; Su, A.; Baugh, E.; Butterfoss, G.L.; Makhatadze, G.; Bystroff, C.; Gross, R.A.
    Influence of surface charge, binding site residues and glycosylation on Thielavia terrestris cutinase biochemical characteristics (2016), Appl. Microbiol. Biotechnol., 100, 4435-4446 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.74

Cloned(Commentary)

Cloned (Comment) Organism
expression in Komagataella pastoris and Saccharomyces cerevisiae Thermothielavioides terrestris

Crystallization (Commentary)

Crystallization (Comment) Organism
homology modeling of structure Thermothielavioides terrestris

Organism

Organism UniProt Comment Textmining
Thermothielavioides terrestris
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein two putative glycosylation sites are predicted from sequence, complete deglycosylation by PNGaseF Thermothielavioides terrestris

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl butanoate + H2O
-
 Thermothielavioides terrestris 4-nitrophenol + butanoate
-
 ?
poly(caprolactone) + H2O
-
 Thermothielavioides terrestris ?
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
64
-
 melting temperature, unglycosylated recombinant protein Thermothielavioides terrestris
67
-
 melting temperature, glycosylated recombinant protein Thermothielavioides terrestris

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
 substrate poly(caprolactone) , recombinant glycosylated enzyme Thermothielavioides terrestris
5 8 broad, substrate 4-nitrophenyl butanoate Thermothielavioides terrestris