Human urinary prokallikrein--structural analysis on activation mechanism.
The complete amino acid sequence of human urinary kallikrein has been determined. The enzyme was a single polypeptide which comprised 238 amino acid residues. In the case of prokallikrein, a propeptide which was consisted of seven amino acid residues was attached to N-terminal isoleucine of kallikrein. The sequence of Asn-X-Thr(Ser), common to glycosylation site, was identified at positions 78-80, 84-86 and 141-143. It has been shown from the sequence of kallikrein that Arg(-1)-Ile(1) and Arg(87)-Gln(88) bonds are hydrolyzed with trypsin on rapid activation of prokallikrein and the formation of disulfide-linked two chain kallikrein.
Takahashi
S
S
Department of Biochemistry, National Cardiovascular Center Research Institute, Osaka, Japan.
Irie
A
A
Katayama
Y
Y
Miyake
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D003488:Cyanogen Bromide; D004789:Enzyme Activation; D004792:Enzyme Precursors / Q000235:genetics*; D006801:Humans; D007610:Kallikreins / Q000235:genetics*; D008969:Molecular Sequence Data; D010179:Pancreas / Q000201:enzymology; D010446:Peptide Fragments / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid; D013552:Swine; D014357:Trypsin
D004792:Enzyme Precursors; D010446:Peptide Fragments; D007610:Kallikreins; C052910:prokallikrein, tissue; D014357:Trypsin; D003488:Cyanogen Bromide