A thermostable promiscuous glucose -1 -phosphate uridyltransferase from Helicobacter pylori for the synthesis of nucleotide sugars
- Author
- MIZANUR, Rahman M1 ; POHL, Nicola L1
[1] Department of Chemistry and the Plant Sciences Institute, Iowa State University, Ames, IA 50011, United States - Source
Journal of molecular catalysis. B, Enzymatic. 2008, Vol 50, Num 1, pp 13-19, 7 p ; ref : 49 ref
- ISSN
- 1381-1177
- Scientific domain
- Biotechnology
- Publisher
- Elsevier Science, Amsterdam
- Publication country
- Netherlands
- Document type
- Article
- Language
- English
- Author keyword
- Charged amino acids Helicobacter pylori Mesophile Nucleotidyltransferase Thermostability
- Keyword (fr)
- Aminoacide Helicobacter pylori Mésophilie Nucleotidyltransferases Nucléotide Stabilité thermique Sucre Synthèse enzymatique α-D-Glucose-1-phosphate uridyltransferase Bactérie Enzyme Spirillaceae Spirillales Transferases
- Keyword (en)
- Aminoacid Helicobacter pylori Mesophily Nucleotidyltransferases Nucleotide Thermal stability Sugar Enzymatic synthesis Bacteria Enzyme Spirillaceae Spirillales Transferases
- Keyword (es)
- Aminoácido Helicobacter pylori Mesofilia Nucleotidyltransferases Nucleótido Estabilidad térmica Azúcar Síntesis enzimática Bacteria Enzima Spirillaceae Spirillales Transferases
- Classification
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A31 Biotechnology / 002A31C Methods. Procedures. Technologies / 002A31C06 Bioconversions. Hemisynthesis
- Discipline
- Biotechnology
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 19881436
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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DOI
10.1016/j.molcatb.2007.09.018 
https://dx.doi.org/10.1016/j.molcatb.2007.09.018
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