******************************************** * Alpha-lactalbumin / lysozyme C signature * ******************************************** Alpha-lactalbumin [1], a milk protein, is the regulatory subunit of lactose synthetase. In the mammary gland, alpha-lactalbumin changes the substrate specificity of galactosyltransferase from N-acetylglucosamine to glucose. Lysozymes (EC 3.2.1.17) [2] act as bacteriolytic enzymes by hydrolyzing the beta(1->4) bonds between N-acetylglucosamine and N-acetylmuramic acid in the peptidoglycan of prokaryotic cell walls. There are at least five different classes of lysozymes [3,4]: C (chicken type), G (goose type), phage-type (T4), fungi (Chalaropsis), and bacterial (Bacillus subtilis) but there are few similarities in the sequences of the different types of lysozymes. Alpha-lactalbumin and lysozyme C are evolutionary related [5]. Around 35 to 40% of the residues are conserved in both proteins as well as the positions of the four disulfide bonds (see the schematic representation). The pattern for this family of proteins includes three cysteines involved in two of these disulfide bonds (the first cysteine is linked to the third one). +-------+ | **|******* xxCxxxxxxxxxxCxxxxxxxxxxxxxxxCxxxxxCxCxxxxxxCxxxxxxxxxCxxxCxx | | +--------+ | | | +----------------------------------------+ | +--------------------------------------------------------+ 'C': conserved cysteine involved in a disulfide bond. '*': position of the pattern. -Consensus pattern: C-x(3)-C-x(2)-[LF]-x(3)-[DEN]-[LI]-x(5)-C -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in SWISS-PROT: NONE. -Note: these proteins belong to family 22 in the classification of glycosyl hydrolases [6]. -Last update: December 1992 / Text revised. [ 1] Hall L., Campbell P.N. Essays Biochem. 22:1-26(1986). [ 2] Concise Encyclopedia Biochemistry, Second Edition, Walter de Gruyter, Berlin New-York (1988). [ 3] Weaver L.H., Grutter M.G., Remington S.J., Gray T.M., Isaacs N.W., Matthews B.W. J. Mol. Evol. 21:97-111(1985). [ 4] Kamei K., Hara S., Ikenaka T., Murao S. J. Biochem. 104:832-836(1988). [ 5] Nitta K., Sugai S. Eur. J. Biochem. 182:111-118(1989). [ 6] Henrissat B. Biochem. J. 280:309-316(1991).