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Literature summary for 3.1.2.20 extracted from

  • Kotowska, M.; Pawlik, K.; Smulczyk-Krawczyszyn, A.; Bartosz-Bechowski, H.; Kuczek, K.
    Type II thioesterase ScoT, associated with Streptomyces coelicolor A3(2) modular polyketide synthase Cpk, hydrolyzes acyl residues and has a preference for propionate (2009), Appl. Environ. Microbiol., 75, 887-896.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
isopropyl-thio-beta-D-galactoside inducer Streptomyces coelicolor

Cloned(Commentary)

Cloned (Comment) Organism
wild-type ScoT and the H224Y mutant expressed in Escherichia coli BL21(DE3)/pLysS cells. Mutants S90A and S90C expressed in Escherichia coli strain BL21Star(DE3). Mutant H210Y expressed in Escherichia coli BL21Star(DE3) cells additionally transformed with plasmid pGroESL encoding chaperones Streptomyces coelicolor

Protein Variants

Protein Variants Comment Organism
H210Y activity is close to that of the wild-type Streptomyces coelicolor
H224Y activity is much lower than that of the wild-type Streptomyces coelicolor
S90A completely abolishes the hydrolytic activity of ScoT Streptomyces coelicolor
S90C exhibits some residual activity Streptomyces coelicolor

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
34
-
N-acetylcysteamine acetate at pH 7.5, 30°C Streptomyces coelicolor
52
-
N-acetylcysteamine propionate at pH 7.5, 30°C Streptomyces coelicolor
56
-
N-acetylcysteamine butyrate at pH 7.5, 30°C Streptomyces coelicolor

Organism

Organism UniProt Comment Textmining
Streptomyces coelicolor
-
-
-

Purification (Commentary)

Purification (Comment) Organism
by nickel affinity chromatography followed by anion-exchange chromatography Streptomyces coelicolor

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information ScoT associated with polyketide synthase Cpk from Streptomyces coelicolor A3 is able to hydrolyze acetyl, propionyl, and butyryl residues. ScoT is an alpha/beta hydrolase with Ser90 and His224 in its active site and it clearly prefers propionate Streptomyces coelicolor ?
-
?
N-acetylcysteamine acetate
-
Streptomyces coelicolor N-acetylcysteamine + acetate
-
?
N-acetylcysteamine butyrate
-
Streptomyces coelicolor N-acetylcysteamine + butyrate
-
?
N-acetylcysteamine propionate
-
Streptomyces coelicolor N-acetylcysteamine + propionate
-
?
p-nitrophenyl acetate + H2O
-
Streptomyces coelicolor p-nitrophenol + acetate
-
?
p-nitrophenyl butyrate
-
Streptomyces coelicolor p-nitrophenol + butyrate
-
?
p-nitrophenyl propionate
-
Streptomyces coelicolor p-nitrophenol + propionate
-
?

Synonyms

Synonyms Comment Organism
SCOT
-
Streptomyces coelicolor
TE II
-
Streptomyces coelicolor
type II thioesterase
-
Streptomyces coelicolor

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.9
-
N-acetylcysteamine propionate at pH 7.5, 30°C Streptomyces coelicolor
1.817
-
N-acetylcysteamine butyrate at pH 7.5, 30°C Streptomyces coelicolor
7.5
-
N-acetylcysteamine acetate at pH 7.5, 30°C Streptomyces coelicolor