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Literature summary for 3.1.1.42 extracted from

  • Nieter, A.; Kelle, S.; Takenberg, M.; Linke, D.; Bunzel, M.; Popper, L.; Berger, R.G.
    Heterologous production and characterization of a chlorogenate esterase from Ustilago maydis with a potential use in baking (2016), Food Chem., 209, 1-9 .
    View publication on PubMed
Search for more literature for 3.1.1.42

Application

Application Comment Organism
food industry the treatment of the wheat dough with the recombinant enzyme causes a softening. The enzyme does not increase the specific bread volume, but improves dough handling. The enzyme may be effective to improve the taste and digestibility of coffee beverages Ustilago maydis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Ustilago maydis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0263
-
 chlorogenate pH 7.5, 37°C Ustilago maydis
0.1251
-
 methyl caffeate pH 7.5, 37°C Ustilago maydis
0.1796
-
 methyl ferulate pH 7.5, 37°C Ustilago maydis
0.2342
-
 methyl p-coumarate pH 7.5, 37°C Ustilago maydis

Organism

Organism UniProt Comment Textmining
Ustilago maydis A0A060S684
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein treatment with endoglycosidase H decreases molecular mass from 87000 Da to 63000 Da Ustilago maydis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
6.38
-
 substrate chlorogenate, pH 7.5, 37°C Ustilago maydis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
alpha-L-galactopyranosyl-(1,2)-beta-D-xylopyranosyl-(1,2)-5-O-trans-feruloyl-L-arabinofuranose + H2O 27% of the activity with chlorogenate Ustilago maydis ?
-
 ?
beta-D-xylopyranosyl-(1,2)-5-O-trans-feruloyl-L-arabinofuranose + H2O 54% of the activity with chlorogenate Ustilago maydis ?
-
 ?
chlorogenate + H2O
-
 Ustilago maydis caffeate + quinate
-
 ?
D-xylopyranosyl-(1,4)-beta-D-xylopyranosyl-(1,3)-5-O-trans-feruloyl-L-arabinofuranose + H2O 38% of the activity with chlorogenate Ustilago maydis ?
-
 ?
ethyl ferulate + H2O 28% of the activity with chlorogenate Ustilago maydis ethanol + ferulate
-
 ?
L-arabinose 5-feruloyl ester + H2O 63% of the activity with chlorogenate Ustilago maydis L-arabinose + ferluate
-
 ?
methyl caffeate + H2O 15% of the activity with chlorogenate Ustilago maydis methanol + caffeate
-
 ?
methyl ferulate + H2O 35% of the activity with chlorogenate Ustilago maydis methanol + ferulate
-
 ?
methyl p-coumarate + H2O 37% of the activity with chlorogenate Ustilago maydis methanol + p-coumarate
-
 ?

Subunits

Subunits Comment Organism
? x * 87000, SDS-PAGE, x * 62300, calculated from sequence, His-tagged recombinant protein Ustilago maydis

Synonyms

Synonyms Comment Organism
chlE
-
 Ustilago maydis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
37
-
 1 h, 20% loss of activity Ustilago maydis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.9
-
 methyl caffeate pH 7.5, 37°C Ustilago maydis
7.1
-
 methyl ferulate pH 7.5, 37°C Ustilago maydis
7.3
-
 methyl p-coumarate pH 7.5, 37°C Ustilago maydis
19
-
 chlorogenate pH 7.5, 37°C Ustilago maydis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Ustilago maydis

pH Stability

pH Stability pH Stability Maximum Comment Organism
2 10 recombinant enzyme, stable over the entire pH range examined Ustilago maydis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
14.8
-
 methyl caffeate pH 7.5, 37°C Ustilago maydis
31
-
 methyl p-coumarate pH 7.5, 37°C Ustilago maydis
39.3
-
 methyl ferulate pH 7.5, 37°C Ustilago maydis
723.3
-
 chlorogenate pH 7.5, 37°C Ustilago maydis