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Literature summary extracted from

  • Ashida, H.; Tanigawa, K.; Kiyohara, M.; Katoh, T.; Katayama, T.; Yamamoto, K.
    Bifunctional properties and characterization of a novel sialidase with esterase activity from Bifidobacterium bifidum (2018), Biosci. Biotechnol. Biochem., 82, 2030-2039 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.53 expression in Escherichia coli Bifidobacterium bifidum
3.2.1.18 expressed in Escherichia coli BL21(lambdaDE3) cells Bifidobacterium bifidum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.53 Cu2+ 5 mM, 30% residual activity Bifidobacterium bifidum
3.1.1.53 additional information not inhibitory: Ca2+, Zn2+, Co2+, Mn2+ and Mg2+ or EDTA Bifidobacterium bifidum
3.2.1.18 Cu2+ 30% residual activity at 5 mM Bifidobacterium bifidum
3.2.1.18 additional information EDTA has no significant effect on the enzyme activity Bifidobacterium bifidum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.18 0.28
-
 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid at pH 5.0 and 37°C Bifidobacterium bifidum

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.53 extracellular extracellular membrane-anchored protein Bifidobacterium bifidum
-
-
3.1.1.53 membrane extracellular membrane-anchored protein Bifidobacterium bifidum 16020
-
3.2.1.18 extracellular
-
 Bifidobacterium bifidum
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.18 additional information Ca2+, Zn2+, Co2+, Mn2+ and Mg2+ have no significant effect on the enzyme activity Bifidobacterium bifidum

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.18 463000
-
 gel filtration Bifidobacterium bifidum

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.53 Bifidobacterium bifidum N0DNS0 bifunctional enzyme, glycoside hydrolase family 33 member. SiaBb1 preferentially hydrolyzes alpha2,3-linked sialic acid from sialoglycan, reaction of EC 3.2.1.18, and has an SGNH hydrolase domain with sialate-O-acetylesterase activity
-
3.2.1.18 Bifidobacterium bifidum
-
-
-
3.2.1.18 Bifidobacterium bifidum JCM1254
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.18 Ni-NTA column chromatography and Superdex 200 gel filtration Bifidobacterium bifidum

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.18 0.00495
-
 with 4-nitrophenyl acetate as substrate, at pH 5.0 and 37°C Bifidobacterium bifidum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.53 4-nitrophenyl acetate + H2O
-
 Bifidobacterium bifidum 4-nitrophenol + acetate
-
 ?
3.1.1.53 5-N-acetyl-9-O-acetylneuraminic acid + H2O
-
 Bifidobacterium bifidum 5-N-acetylneuraminic acid + acetate
-
 ?
3.2.1.18 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O
-
 Bifidobacterium bifidum 4-methylumbelliferone + alpha-D-N-acetylneuraminic acid
-
 ?
3.2.1.18 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid + H2O
-
 Bifidobacterium bifidum JCM1254 4-methylumbelliferone + alpha-D-N-acetylneuraminic acid
-
 ?
3.2.1.18 4-nitrophenyl acetate + H2O
-
 Bifidobacterium bifidum 4-nitrophenol + acetate
-
 ?
3.2.1.18 4-nitrophenyl acetate + H2O
-
 Bifidobacterium bifidum JCM1254 4-nitrophenol + acetate
-
 ?
3.2.1.18 additional information isoform SiaBb1 preferentially hydrolyzes alpah2,3-linked sialic acid over alpha2,6-linked sialic acid from sialoglycan. Isoform SiaBb1 also has an SGNH hydrolase domain with sialate-O-acetylesterase activity Bifidobacterium bifidum ?
-
 ?
3.2.1.18 additional information no activity with 4-nitrophenyl butyrate, 4-nitrophenyl valerate, 4-nitrophenyl decanoate, 4-nitrophenyl palmitate, and 4-nitrophenyl phosphate Bifidobacterium bifidum ?
-
 ?
3.2.1.18 additional information isoform SiaBb1 preferentially hydrolyzes alpah2,3-linked sialic acid over alpha2,6-linked sialic acid from sialoglycan. Isoform SiaBb1 also has an SGNH hydrolase domain with sialate-O-acetylesterase activity Bifidobacterium bifidum JCM1254 ?
-
 ?
3.2.1.18 additional information no activity with 4-nitrophenyl butyrate, 4-nitrophenyl valerate, 4-nitrophenyl decanoate, 4-nitrophenyl palmitate, and 4-nitrophenyl phosphate Bifidobacterium bifidum JCM1254 ?
-
 ?
3.2.1.18 mucin of bovine submaxillary gland + H2O
-
 Bifidobacterium bifidum sialic acid + ?
-
 ?
3.2.1.18 mucin of bovine submaxillary gland + H2O
-
 Bifidobacterium bifidum JCM1254 sialic acid + ?
-
 ?
3.2.1.18 pyridylamino-3'-sialyllactose + H2O
-
 Bifidobacterium bifidum ?
-
 ?
3.2.1.18 pyridylamino-6'-sialyllactose + H2O
-
 Bifidobacterium bifidum ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.53 ? x * 1898000, calculated from sequence, xy * 190000, SDS-PAGE Bifidobacterium bifidum
3.2.1.18 homodimer 2 * 190000, SDS-PAGE Bifidobacterium bifidum

Synonyms

EC Number Synonyms Comment Organism
3.1.1.53 SiaBb1
-
 Bifidobacterium bifidum
3.2.1.18 SiaBb1
-
 Bifidobacterium bifidum
3.2.1.18 sialyl hydrolase
-
 Bifidobacterium bifidum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.53 40 45
-
 Bifidobacterium bifidum
3.2.1.18 40 45
-
 Bifidobacterium bifidum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.53 40
-
 stable below Bifidobacterium bifidum
3.2.1.18 40
-
 the enzyme is stable at temperatures less than 40°C Bifidobacterium bifidum

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.18 33
-
 4-methylumbelliferyl alpha-D-N-acetylneuraminic acid at pH 5.0 and 37°C Bifidobacterium bifidum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.53 4.5
-
-
 Bifidobacterium bifidum
3.2.1.18 4.5
-
-
 Bifidobacterium bifidum

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.53 6 9
-
 Bifidobacterium bifidum
3.2.1.18 6 9 the enzyme is stable over the pH range of 6.0-9.0 Bifidobacterium bifidum

General Information

EC Number General Information Comment Organism
3.1.1.53 physiological function a SiaBb1 construct that lacks the SGNH hydrolase and Lam G domains cannot catalyze 4-nitrophenyl acetate hydrolysis, but retains sialidase activity Bifidobacterium bifidum