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Literature summary for 3.2.1.37 extracted from

  • Dong, B.; Luo, H.; Liu, B.; Li, W.; Ou, S.; Wu, Y.; Zhang, X.; Pang, X.; Zhang, Z.
    BcXyl, a beta-xylosidase isolated from Brunfelsia calycina flowers with anthocyanin-beta-glycosidase activity (2019), Int. J. Mol. Sci., 20, 1423 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.2.1.37

Cloned(Commentary)

Cloned (Comment) Organism
-
 Brunfelsia pauciflora var. calycina

Inhibitors

Inhibitors Comment Organism Structure
Ag+ 1 mM, 88% inhibition Brunfelsia pauciflora var. calycina
D-gluconate 1 mM, 87% inhibition Brunfelsia pauciflora var. calycina
Hg2+ 1 mM, 40% inhibition Brunfelsia pauciflora var. calycina
additional information 10 mM Mg2+, Cu2+, Mn2+ and Ca2+ show no inhibition Brunfelsia pauciflora var. calycina

Organism

Organism UniProt Comment Textmining
Brunfelsia pauciflora var. calycina
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Brunfelsia pauciflora var. calycina

Source Tissue

Source Tissue Comment Organism Textmining
flower
-
 Brunfelsia pauciflora var. calycina
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl beta-D-galactopyranoside + H2O
-
 Brunfelsia pauciflora var. calycina 4-nitrophenol + beta-D-galactose
-
 ?
4-nitrophenyl beta-D-xylopyranoside + H2O 39.36% of the activitzy compared to 4-nitrophenyl beta-D-galactopyranoside Brunfelsia pauciflora var. calycina 4-nitrophenol + beta-D-xylose
-
 ?
anthocyanin + H2O the enzyme catalyzes the degradation of an anthocyanin component of Brunfelsia calycina, and the release of xylose and galactose due to hydrolysis of glycosidic bonds by BcXyl is detected Brunfelsia pauciflora var. calycina ?
-
 ?
additional information no activity to 4-nitrophenyl beta-D-glucopyranoside or 4-nitrophenyl-beta-D-mannopyranoside. Based on fragment sequences of the enzyme detected by tandem mass spectrometry and their identical hits from other plant species the purified enzyme is a beta-xylosidase Brunfelsia pauciflora var. calycina ?
-
 ?

Synonyms

Synonyms Comment Organism
BcXyl
-
 Brunfelsia pauciflora var. calycina

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Brunfelsia pauciflora var. calycina

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 50 30°C: about 55% of maximal activity, 50°C: about 75% of maximal activity Brunfelsia pauciflora var. calycina

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Brunfelsia pauciflora var. calycina

pH Range

pH Minimum pH Maximum Comment Organism
4 6 pH 4.0: about 45% of maximal activity, pH 6.0: about 62% of maximal activity Brunfelsia pauciflora var. calycina

General Information

General Information Comment Organism
physiological function the enzyme catalyzes the degradation of an anthocyanin component of Brunfelsia calycina, and the release of xylose and galactose due to hydrolysis of glycosidic bonds by BcXyl is detected. The enzyme is activated at the stage at which the rapid anthocyanin degradation occurrs Brunfelsia pauciflora var. calycina