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Literature summary for 3.2.1.52 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)

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 ?
-
?
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

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

Purification (Commentary)

Purification (Comment) Organism
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]

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl N-acetyl-beta-D-galactosamine + H2O
-
Lactococcus lactis 4-nitrophenol + N-acetyl-beta-galactosamine
-
?
4-nitrophenyl N-acetyl-beta-D-galactosamine + H2O
-
Lactococcus lactis IL1403 4-nitrophenol + N-acetyl-beta-galactosamine
-
?
4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
-
Lactococcus lactis 4-nitrophenol + N-acetyl-beta-glucosamine
-
?
4-nitrophenyl N-acetyl-beta-D-glucosamine + H2O
-
Lactococcus lactis IL1403 4-nitrophenol + N-acetyl-beta-glucosamine
-
?
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 ?
-
?
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 ?
-
?
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 ?
-
?
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

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

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
-
-
Lactococcus lactis

pH Range

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

pH Stability

pH Stability pH Stability Maximum Comment Organism
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

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