Isolation and characterization of three serine protease genes in the mosquito Anopheles gambiae.
Three genes encoding serine proteases (Sp6A, Sp6T and Sp8T) were isolated from the malaria mosquito An. gambiae. The proteins that are conceptually translated from these genes contain all amino acids that have been described for this class of proteolytic enzymes, namely the His, Asp and Ser residues at the active site, and the six cysteine residues that form the three disulphide bridges in invertebrate serine proteases. The genes are expressed at low levels and the transcripts were detected only by PCR. Analysis of the nucleotide sequences of the three genes and their pattern of expression indicate that none of the genes code for digestive enzymes, but rather that the proteins have features of the tethered type of serine proteases.
Sidén-Kiamos
I
I
Insititute for Molecular Biology and Biotechnology, Foundation for Research and Technology-Hellas, Heraklion, Greece.
Skavdis
G
G
Rubio
J
J
Papaginnakis
G
G
Louis
C
C
D000595:Amino Acid Sequence; D000818:Animals; D000852:Anopheles / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D004247:DNA; D015870:Gene Expression; D017344:Genes, Insect; D006801:Humans; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000235:genetics*
D004247:DNA; D012697:Serine Endopeptidases