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Literature summary extracted from

  • Nguyen, H.A.; Nguyen, T.H.; K?en, V.; Eijsink, V.G.; Haltrich, D.; Peterbauer, C.K.
    Heterologous expression and characterization of an N-acetyl-beta-D-hexosaminidase from Lactococcus lactis ssp. lactis IL1403 (2012), J. Agric. Food Chem., 60, 3275-3281.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.52 gene lnbA, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) Lactococcus lactis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.52 Ca2+ 37% inhibition at 1 mM, 73% at 50 mM Lactococcus lactis
3.2.1.52 Cu2+ complete inhibition at 1-50 mM Lactococcus lactis
3.2.1.52 Fe3+ 65% inhibition at 1 mM, complete at 50 mM Lactococcus lactis
3.2.1.52 Mg2+ slightly inhibitory at 1-50 mM Lactococcus lactis
3.2.1.52 Mn2+ 85% inhibition at 1-50 mM Lactococcus lactis
3.2.1.52 Zn2+ 42% inhibition at 1 mM, 87% at 50 mM Lactococcus lactis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.52 2.56
-
 4-nitrophenyl N-acetyl-beta-D-glucosamine pH 6.0, 37°C Lactococcus lactis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.52 K+ slightly activating at 1-50 mM Lactococcus lactis
3.2.1.52 Na+ slightly activating at 1-50 mM Lactococcus lactis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.52 additional information Lactococcus lactis the enzyme shows hydrolytic activity on chito-oligosaccharides but not on colloidal chitin or chitosan, it has both N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase activity, thus indicating that the enzyme is an N-acetyl-beta-D-hexosaminidase ?
-
 ?
3.2.1.52 additional information Lactococcus lactis IL1403 the enzyme shows hydrolytic activity on chito-oligosaccharides but not on colloidal chitin or chitosan, it has both N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase activity, thus indicating that the enzyme is an N-acetyl-beta-D-hexosaminidase ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.52 Lactococcus lactis Q9CFI2 ssp. lactis, gene lnbA
-
3.2.1.52 Lactococcus lactis IL1403 Q9CFI2 ssp. lactis, gene lnbA
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.52 gene lnbA, recombinant His6-tagged enzyme about 2fold from Escherichia coli strain BL21(DE3) by ultrafiltration, nickel affinity chromatography, dialysis and ultrafiltration Lactococcus lactis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.52 19.1
-
 crude recombinant enzyme, pH 6.0, 37°C, substrate 4-nitrophenyl N-acetyl-beta-D-glucosamine Lactococcus lactis
3.2.1.52 37
-
 purified recombinant enzyme, pH 6.0, 37°C, substrate 4-nitrophenyl N-acetyl-beta-D-glucosamine Lactococcus lactis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.52 4-nitrophenyl N-acetyl-beta-D-galactosamine + H2O
-
 Lactococcus lactis 4-nitrophenol + N-acetyl-beta-galactosamine
-
 ?
3.2.1.52 4-nitrophenyl N-acetyl-beta-D-galactosamine + H2O
-
 Lactococcus lactis IL1403 4-nitrophenol + N-acetyl-beta-galactosamine
-
 ?
3.2.1.52 4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
-
 Lactococcus lactis 4-nitrophenol + N-acetyl-beta-glucosamine
-
 ?
3.2.1.52 4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
-
 Lactococcus lactis IL1403 4-nitrophenol + N-acetyl-beta-glucosamine
-
 ?
3.2.1.52 additional information the enzyme shows hydrolytic activity on chito-oligosaccharides but not on colloidal chitin or chitosan, it has both N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase activity, thus indicating that the enzyme is an N-acetyl-beta-D-hexosaminidase Lactococcus lactis ?
-
 ?
3.2.1.52 additional information substrate specificity analysis, no significant activity with 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-arabinopyranoside, 4-nitrophenyl beta-D-xylopyranoside, 4-nitrophenyl 6-O-sulfo-N-acetyl-beta-D-glucosaminide, 2-acetamido-2-deoxy-beta-D-glucopyranosylazide, 2-acetamido-2-deoxy-beta-D-glucopyranourate, colloidal chitin, and chitosan Lactococcus lactis ?
-
 ?
3.2.1.52 additional information the enzyme shows hydrolytic activity on chito-oligosaccharides but not on colloidal chitin or chitosan, it has both N-acetyl-beta-D-glucosaminidase and N-acetyl-beta-D-galactosaminidase activity, thus indicating that the enzyme is an N-acetyl-beta-D-hexosaminidase Lactococcus lactis IL1403 ?
-
 ?
3.2.1.52 additional information substrate specificity analysis, no significant activity with 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl beta-D-arabinopyranoside, 4-nitrophenyl beta-D-xylopyranoside, 4-nitrophenyl 6-O-sulfo-N-acetyl-beta-D-glucosaminide, 2-acetamido-2-deoxy-beta-D-glucopyranosylazide, 2-acetamido-2-deoxy-beta-D-glucopyranourate, colloidal chitin, and chitosan Lactococcus lactis IL1403 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.52 beta-NAHA
-
 Lactococcus lactis
3.2.1.52 lacto-N-biosidase UniProt Lactococcus lactis
3.2.1.52 lnba
-
 Lactococcus lactis
3.2.1.52 N-acetyl-beta-D-hexosaminidase
-
 Lactococcus lactis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.52 37
-
-
 Lactococcus lactis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.52 20 55 activity range, profile overview Lactococcus lactis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.52 37
-
 purified enzyme, pH 6.0, half-life is 53 h Lactococcus lactis
3.2.1.52 50
-
 purified enzyme, pH 6.0, 30 min, inactivation Lactococcus lactis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.2.1.52 26.7
-
 4-nitrophenyl N-acetyl-beta-D-glucosamine pH 6.0, 37°C Lactococcus lactis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.52 5.5
-
-
 Lactococcus lactis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.52 4.5 8 activity range, profile overview Lactococcus lactis

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.52 5.5 8 purified enzyme, 37°C, 30 min: over 80% activity remaining, 24 h: 40% activity remaining at pH 5.5, over 80% at pH 6.0-7.0, 30% at pH 8.0, unstable below pH 5.5, residual activity after 30 min incubation at pH 4.0-5.0 is below 20% Lactococcus lactis

General Information

EC Number General Information Comment Organism
3.2.1.52 physiological function the enzyme may be responsible for degrading chito-oligosaccharides that are produced by the chitinolytic system of Lactobacillus lactis Lactococcus lactis