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Literature summary for 3.1.1.6 extracted from

  • Li, X.L.; Skory, C.D.; Cotta, M.A.; Puchart, V.; Biely, P.
    Novel family of carbohydrate esterases, based on identification of the Hypocrea jecorina acetyl esterase gene (2008), Appl. Environ. Microbiol., 74, 7482-7489.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.6

Activating Compound

Activating Compound Comment Organism Structure
cellobiose enhanced activity with 4-nitrophenyl acetate as substrate Trichoderma reesei
D-galactose enhanced activity with 4-nitrophenyl acetate as substrate Trichoderma reesei
D-glucose 1% (w/v), enhanced activity with 4-nitrophenyl acetate as substrate Trichoderma reesei
D-xylose at high concentrations of 10-500 mM, enhanced activity with 4-nitrophenyl acetate as substrate Trichoderma reesei
additional information no influence on activity on 4-nitrophenyl acetate as substrate by L-arabinose, mannose, lactose Trichoderma reesei
additional information rates of hydrolysis of 4-nitrophenyl acetate by the purified Aes1 are inhibited by low concentrations (1.0 to 5.0 mM) but significantly enhanced by high concentrations (10.0 to 500 mM) of D-xylose Trichoderma reesei
additional information sodium acetate at concentrations below 100 mM does not inhibit the hydrolysis, higher concentrations inhibit the reactions Trichoderma reesei
additional information using 4-nitrophenyl acetate as substrate the activity of the recombinant enzyme is enhanced by D-xylose, D-glucose, cellobiose, D-galactose, and xylooligosaccharides but not by arabinose, mannose, or lactose Trichoderma reesei
xylooligosaccharide 50 mM, enhanced activity with 4-nitrophenyl acetate as substrate Trichoderma reesei

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli DH5 alpha Trichoderma reesei
from genomic DNA in pT3C to generate expression plasmid pTSP-TAE and transformation of Hypocrea jecorina Rut-C30 Trichoderma reesei

Inhibitors

Inhibitors Comment Organism Structure
D-xylose at low concentrations of 1-5 mM, altered activity with 4-nitrophenyl acetate as substrate Trichoderma reesei
additional information rates of hydrolysis of 4-nitrophenyl acetate by the purified Aes1 are inhibited by low concentrations (1.0 to 5.0 mM) but significantly enhanced by high concentrations (10.0 to 500 mM) of D-xylose Trichoderma reesei
Sodium acetate at concentrations higher than 100 mM Trichoderma reesei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.23
-
 4-nitrophenyl acetate 30°C, pH 5.8 Trichoderma reesei
0.23
-
 4-nitrophenyl acetate purified recombinant enzyme, 30°C, pH 5.8 Trichoderma reesei

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Trichoderma reesei
-
-
extracellular 19 N-terminal residues serve as signal peptide for secretion Trichoderma reesei
-
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37090
-
 theoretical, polypeptide of 348 amino acids Trichoderma reesei
42000
-
 over-expression in Hypocrea jecorina Rut-C30, SDS-PAGE, molecular weight shift of purified recombinant enzyme (below theoretical weight) upon treatment with endoglycosidase H Trichoderma reesei
45000
-
 SDS-PAGE Trichoderma reesei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Trichoderma reesei new family of microbial esterases with hemicellulase activity for biodegradation of lignocellulose, complementary activity to acetylxylan esterase Axe1 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Trichoderma reesei A7J2C6 anamorph Trichoderma reesei, strain Rut-C30 (hypercellulolytic mutant of Trichoderma reesei QM 6a)
-
Trichoderma reesei A7J2C6 Trichoderma reesei strain ATCC 56765
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein N-glycosylation, sensitive to endoglycosidase H but not to O-glycosidase treatment, putative acceptor sites: N45, N146, N198, N204, N278 Trichoderma reesei

Purification (Commentary)

Purification (Comment) Organism
after over-expression (up to 20fold activity) by liquid column chromatography, monitored by activity measurements, 300 mg recombinant enzyme from 1 litre culture Trichoderma reesei
centrifugation at 4°C, liquid column chromatography Trichoderma reesei

Source Tissue

Source Tissue Comment Organism Textmining
culture supernatant
-
 Trichoderma reesei
-
mycelium high transcript level induced by 4 mM sophorose, 1% (w/v) cellulose, 1% (w/v) oat spelt xylan, or 1% (w/v) lactose, significant transcript levels induced by 1% (w/v) L-arabinose, low transcript levels induced by acetic acid (4 mM sodium acetate, 1% (w/v) glycerol), revealed by Northern blot Trichoderma reesei
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 extremly low activities against 4-nitrophenyl formate, butyrate, or canoate Trichoderma reesei
0.000109
-
 4-nitrophenyl butyrate, purified recombinant enzyme Trichoderma reesei
0.000213
-
 4-nitrophenyl formate, purified recombinant enzyme Trichoderma reesei
0.21
-
 4-nitrophenyl acetate, over-expression culture supernatant Trichoderma reesei
0.21
-
 recombinant enzyme, culture supernatant Trichoderma reesei
0.85
-
 recombinant enzyme, after CM Sepharose FF column Trichoderma reesei
1.12
-
 recombinant enzyme, after DEAE FF column, 4-nitrophenyl acetate Trichoderma reesei
1.21
-
 4-nitrophenyl acetate, purified recombinant enzyme Trichoderma reesei
20.5
-
 4-nitrophenyl acetate, maximum velocity, purified recombinant enzyme, 30°C, pH 5.8 Trichoderma reesei

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl acetate + H2O
-
 Trichoderma reesei 4-nitrophenol + acetate
-
 ?
4-nitrophenyl acetate + H2O 5 min, 30°C, pH 5.8, for kinetic analyses: 0.05-5 mM substrate in 100 mM sodium phosphate buffer Trichoderma reesei 4-nitrophenol + acetate analysis by spectrophotometry at 410 nm ?
4-nitrophenyl beta-D-xylopyranoside + H2O 4 mM substrate, position-specificity, hydrolysis activity is specific for 3-, and 4-O-acetyl 4-nitrophenyl-beta-D-xylopyranoside, 2-O-acetyl 4-nitrophenyl-beta-D-xylopyranoside is a bad substrate Trichoderma reesei 4-nitrophenyl D-xylopyranose beta-xylosidase-coupled assay ?
4-nitrophenyl butyrate + H2O 5 min, 30°C, pH 5.8 Trichoderma reesei 4-nitrophenol + butyrate
-
 ?
4-nitrophenyl formate + H2O 5 min, 30°C, pH 5.8 Trichoderma reesei 4-nitrophenol + formate
-
 ?
methyl-beta-D-xylopyranoside + vinylacetate transacetylation of methylxyloside in aqueous solution (40°C, pH 6, 25 mM methyl-beta-D-xylopyranoside) Trichoderma reesei methyl-beta-D-xylopyranoside monoacetate + vinyl alcohol analysis by thin-layer chromatography ?
additional information new family of microbial esterases with hemicellulase activity for biodegradation of lignocellulose, complementary activity to acetylxylan esterase Axe1 Trichoderma reesei ?
-
 ?

Synonyms

Synonyms Comment Organism
Acetyl esterase
-
 Trichoderma reesei
Aes1
-
 Trichoderma reesei
Aes1 encoded by gene aes1, contains GDSY lipase motif Trichoderma reesei
carbohydrate esterase new family, less than 30% identity to carbohydrate esterases of known families Trichoderma reesei

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 4-nitrophenyl-beta-D-xylopyranoside monoacetate initial rate ratio between 2-, 3-, and 4-O-acetyl 4-nitrophenyl-beta-D-xylopyranoside is 1:19:17.7 Trichoderma reesei

pI Value

Organism Comment pI Value Maximum pI Value
Trichoderma reesei theoretical
-
 5.9
Trichoderma reesei purified recombinant enzyme
-
 6