The terminal enzymes of sialic acid metabolism: acylneuraminate pyruvate-lyases.
The acylneuraminate pyruvate-lyase gene from Clostridium perfringens was sequenced and found to be most similar to the lyase gene from Haemophilus influenzae. Both the recombinant clostridial enzyme and the native enzyme from pig kidney were purified in larger amounts and characterized. The properties of the porcine lyase are similar to the microbial ones. However, the much higher degree of similarity in comparison to the microbial enzymes that was found between porcine lyase peptides and two putative mammalian lyase sequences show that the latter form an own group apart from the microbial lyases. Actual models of the acylneuraminate pyruvate-lyase reaction are discussed.
Schauer
R
R
Institute of Biochemistry, Christian-Albrechts-Universität, Kiel, Germany. Schauer@biochem.uni-kiel.de
Sommer
U
U
Krüger
D
D
van Unen
H
H
Traving
C
C
D000595:Amino Acid Sequence; D000818:Animals; D003016:Clostridium perfringens / Q000201:enzymology* / Q000235:genetics; D007668:Kidney / Q000201:enzymology; D008969:Molecular Sequence Data; D019158:N-Acetylneuraminic Acid / Q000378:metabolism*; D007652:Oxo-Acid-Lyases / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D013552:Swine
D007652:Oxo-Acid-Lyases; C018728:N-acetylneuraminate lyase; D019158:N-Acetylneuraminic Acid