Genetic and molecular analyses of Escherichia coli N-acetylneuraminate lyase gene
نویسندگان
چکیده
منابع مشابه
Purification and properties of N-acetylneuraminate lyase from Escherichia coli.
N-Acetylneuraminate lyase [N-acetylneuraminic acid aldolase EC 4.1.3.3] from Escherichia coli was purified by protamine sulfate treatment, fractionation with ammonium sulfate, column chromatography on DEAE-Sephacel, gel filtration on Ultrogel AcA 44, and preparative polyacrylamide gel electrophoresis. The purified enzyme preparation was homogeneous on analytical polyacrylamide gel electrophores...
متن کاملCloning and constitutive expression of the N-acetylneuraminate lyase gene of Escherichia coli.
The N-acetylneuraminate (NANA) lyase (EC 4.1.3.3) gene from Escherichia coli was self-cloned in E. coli. Transformants were selected by complementation of a NANA lyase-deficient E. coli strain. One clone was found to produce NANA lyase, and it contained a recombinant plasmid, pNAL1, with a 9.0-kilobase HindIII insert. The cloning of the NANA lyase gene resulted in the change from inducible to c...
متن کاملPurification, crystallization and characterization of N-acetylneuraminate lyase from Escherichia coli.
N-Acetylneuraminate lyase produced by Escherichia coli was purified and crystallized from a genetically engineered strain (E. coli SF8/pNAL1). The enzyme showed apparent molecular masses of 105,000 Da on gel filtration and 35,000 Da on SDS/PAGE, suggesting that the enzyme is a trimer. The apparent optimum pH and temperature were found to be 6.5-7.0 and 80 degrees C respectively. The Km values f...
متن کاملMolecular characterization of a novel N-acetylneuraminate lyase from Lactobacillus plantarum WCFS1.
N-Acetylneuraminate lyases (NALs) or sialic acid aldolases catalyze the reversible aldol cleavage of N-acetylneuraminic acid (Neu5Ac) to form pyruvate and N-acetyl-d-mannosamine (ManNAc). In nature, N-acetylneuraminate lyase occurs mainly in pathogens. However, this paper describes how an N-acetylneuraminate lyase was cloned from the human gut commensal Lactobacillus plantarum WCFS1 (LpNAL), ov...
متن کاملMolecular Characterization of a Novel N-Acetylneuraminate Lyase from a Deep-Sea Symbiotic Mycoplasma
N-acetylneuraminic acid (Neu5Ac) based novel pharmaceutical agents and diagnostic reagents are highly required in medical fields. However, N-acetylneuraminate lyase（NAL）for Neu5Ac synthesis is not applicable for industry due to its low catalytic efficiency. In this study, we biochemically characterized a deep-sea NAL enzyme (abbreviated form: MyNal) from a symbiotic Mycoplasma inhabiting the st...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1986
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.167.1.404-406.1986