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Literature summary for 3.1.1.72 extracted from

  • Till, M.; Goldstone, D.C.; Attwood, G.T.; Moon, C.D.; Kelly, W.J.; Arcus, V.L.
    Structure and function of an acetyl xylan esterase (Est2A) from the rumen bacterium Butyrivibrio proteoclasticus (2013), Proteins, 81, 911-917.
    View publication on PubMed
Search for more literature for 3.1.1.72

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Butyrivibrio proteoclasticus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinnat wild-type enzyme and mutant H351A, X-ray diffraction structure determination and analysis at 2.1 A and 2.0 A resolution, respectively, single wavelength anomalous diffraction and molecular replacement methods, three-dimensional structure determintaion Butyrivibrio proteoclasticus

Protein Variants

Protein Variants Comment Organism
H351A site-directed mutagenesis, inactive mutant Butyrivibrio proteoclasticus
S142A site-directed mutagenesis Butyrivibrio proteoclasticus

Organism

Organism UniProt Comment Textmining
Butyrivibrio proteoclasticus E0RVY7
-
-
Butyrivibrio proteoclasticus B316 E0RVY7
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by metal chelating nickel affinity chromatography Butyrivibrio proteoclasticus

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl acetate + H2O
-
 Butyrivibrio proteoclasticus 4-nitrophenol + acetate
-
 ?
4-nitrophenyl acetate + H2O
-
 Butyrivibrio proteoclasticus B316 4-nitrophenol + acetate
-
 ?
4-nitrophenyl butyrate + H2O
-
 Butyrivibrio proteoclasticus 4-nitrophenol + butyrate
-
 ?
4-nitrophenyl butyrate + H2O
-
 Butyrivibrio proteoclasticus B316 4-nitrophenol + butyrate
-
 ?

Subunits

Subunits Comment Organism
More the enzyme contains a C-terminal SGNH domain and an N-terminal jelly-roll domain typical of CE2 family structures, three-dimensional structure analysis, overview Butyrivibrio proteoclasticus

Synonyms

Synonyms Comment Organism
acetyl xylan esterase
-
 Butyrivibrio proteoclasticus
Est2A
-
 Butyrivibrio proteoclasticus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Butyrivibrio proteoclasticus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 assay at Butyrivibrio proteoclasticus

General Information

General Information Comment Organism
evolution the enzyme belongs to the carbohydrate esterase family 2, CE2, and has a domain structure typical of CE2 family structures, a C-terminal SGNH domain and an N-terminal jelly-roll domain Butyrivibrio proteoclasticus
additional information the active site of the enzyme is located at the base of a groove lined by two tryptophan residues, Trp158 and Trp195 are arranged in a parallel fashion on either side above the active site Butyrivibrio proteoclasticus