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Literature summary extracted from

  • Mukhopadhyay, A.; Hazra, P.P.; Sengupta, T.; Saha, R.; Nandi, R.; Sengupta, S.
    Protein-protein interaction conferring stability to an extracellular acetyl (xylan) esterase produced by Termitomyces clypeatus (2003), Biotechnol. Prog., 19, 720-726.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.1.72 additional information enzyme is not affected by 2-mercaptoethanol and EDTA Termitomyces clypeatus

General Stability

EC Number General Stability Organism
3.1.1.72 the enzyme aggregated with cellobiase shows higher thermal stability, temperature optimum, and resistance to chemical denaturants than the isolated purified enzyme Termitomyces clypeatus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.72 guanidinium hydrochloride 3.5-4.0 M, inactivation Termitomyces clypeatus
3.1.1.72 additional information no inhibition by xylose and acetate, enzyme is not affected by 2-mercaptoethanol and EDTA Termitomyces clypeatus
3.1.1.72 SDS 0.5% inhibit the single enzyme, but 5% do not affect the aggregated enzyme Termitomyces clypeatus
3.1.1.72 Trypsin single enzyme loses its activity completely after 30 min at 37°C, while the aggregated enzyme shows 75-80% remaining activity after 60 min incubation at 37°C Termitomyces clypeatus
3.1.1.72 Urea 7.0 M, inactivation Termitomyces clypeatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.1.72 0.36
-
 4-nitrophenyl acetate pH 6.5, 50°C Termitomyces clypeatus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.72 extracellular
-
 Termitomyces clypeatus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.72 Fe2+ about 25% activation Termitomyces clypeatus
3.1.1.72 Mg2+ about 25% activation Termitomyces clypeatus
3.1.1.72 additional information enzyme is not affected by Ca2+, Cu2+, and Zn2+ Termitomyces clypeatus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.72 additional information
-
 the enzyme is aggregated with a cellobiase tetramer to form a 80 kDa protein complex Termitomyces clypeatus
3.1.1.72 30000
-
 gel filtration Termitomyces clypeatus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.72 Termitomyces clypeatus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.72 no glycoprotein
-
 Termitomyces clypeatus

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.72 purification of the enzyme as a single 30 kDa protein, 60fold, and aggregated with cellobiase to a 80 kDa protein complex Termitomyces clypeatus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.72 acetylxylan + 3 H2O = 3 acetic acid + xylan catalyses the hydrolysis of acetyl groups from polymeric xylan, acetylated xylose, acetylated glucose, alpha-naphthyl acetate, p-nitrophenyl acetate but not from triacetylglycerol. Does not act on acetylated mannan or pectin. Termitomyces clypeatus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.1.1.72 additional information
-
-
 Termitomyces clypeatus
3.1.1.72 80
-
 purified single enzyme Termitomyces clypeatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.72 4-nitrophenyl acetate + H2O
-
 Termitomyces clypeatus 4-nitrophenol + acetate
-
 ?
3.1.1.72 acetylated xylan + H2O substrate from birchwood Termitomyces clypeatus xylan + acetate
-
 ?
3.1.1.72 additional information alpha-naphthyl acetate is a poor substrate Termitomyces clypeatus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.72 monomer 1 * 30000, SDS-PAGE Termitomyces clypeatus

Synonyms

EC Number Synonyms Comment Organism
3.1.1.72 acetyl (xylan) esterase
-
 Termitomyces clypeatus
3.1.1.72 Acetyl esterase
-
 Termitomyces clypeatus
3.1.1.72 AE
-
 Termitomyces clypeatus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.72 additional information
-
 the temperature optimum is increased by aggregation of the enzyme with cellobiase Termitomyces clypeatus
3.1.1.72 45
-
 single enzyme Termitomyces clypeatus
3.1.1.72 55
-
 aggregated enzyme Termitomyces clypeatus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.72 additional information
-
 the enzyme aggregated with cellobiase shows higher thermal stability than the isolated purified enzyme Termitomyces clypeatus
3.1.1.72 35
-
 single enzyme Termitomyces clypeatus
3.1.1.72 50
-
 30 min, pH 6.5, single enzyme, complete loss of activity Termitomyces clypeatus
3.1.1.72 70
-
 aggregated enzyme Termitomyces clypeatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.72 6.5
-
-
 Termitomyces clypeatus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.72 5 8
-
 Termitomyces clypeatus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.1.1.72 Termitomyces clypeatus chromatocfocusing 7.4 7.3