Heterologous Expression and Characterization of an N-Acetyl-beta-D-hexosaminidase from Lactococcus lactis ssp. lactis IL1403

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F12%3A00377491" target="_blank" >RIV/61388971:_____/12:00377491 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1021/jf204915e" target="_blank" >http://dx.doi.org/10.1021/jf204915e</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/jf204915e" target="_blank" >10.1021/jf204915e</a>

Result language
angličtina
Original language name
Heterologous Expression and Characterization of an N-Acetyl-beta-D-hexosaminidase from Lactococcus lactis ssp. lactis IL1403
Original language description
The lnbA gene of Lactococcus lactis ssp. lactis IL1403 encodes a polypeptide with similarity to lacto-N-biosidases and N-acetyl-beta-D-hexosaminidases. The gene was cloned into the expression vector pET-21d and overexpressed in Escherichia coli BL21* (DE3). The recombinant purified enzyme (LnbA) was a monomer with a molecular weight of approximately 37 kDa. Studies with chromogenic substrates including p-nitrophenyl N-acetyl-beta-D-glucosamine (pNP-GlcNAc) and p-nitrophenyl N-acetyl-beta-D-galactosamine(pNP-GalNAc) showed that the enzyme had 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. K-m and k(cat) for pNP-GlcNAc were 2.56 mM and 26.7 s(-1),respectively, whereas kinetic parameters for pNP-GalNAc could not be determined due to the Km being very high (>10 mM)
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CE - Biochemistry
OECD FORD branch
—

Project
<a href="/en/project/GAP207%2F11%2F0629" target="_blank" >GAP207/11/0629: Thiazoline inhibitors of ?-N-acetylhexosaminidase based on new, non-natural substrates.</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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