Cathepsin L-like protease from Xenopus embryos that is stimulated by nucleoside phosphates and nucleic acids.
An acid thiol protease that was activated at an early stage of embryogenesis was purified from Xenopus embryos. The N-terminal amino acid sequence (16 residues) of the heavy chain of the enzyme was similar to that of cathepsin L. The proteolytic activity of the protease was enhanced by ATP. Other nucleoside triphosphates, AMP and nucleic acids also enhanced the proteolytic activity. The possible mechanism and biological significance of the activation of the protease in Xenopus embryos are discussed.
Miyata
S
S
Department of Chemistry, College of Humanities and Sciences, Nihon University, Tokyo, Japan.
Kihara
H K
HK
D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000595:Amino Acid Sequence; D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000187:drug effects / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000378:metabolism*; D004247:DNA / Q000494:pharmacology; D004625:Embryo, Nonmammalian / Q000201:enzymology*; D010450:Endopeptidases; D004789:Enzyme Activation; D006454:Hemoglobins / Q000378:metabolism; D006657:Histones / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D012709:Serum Albumin / Q000378:metabolism; D014981:Xenopus
D006454:Hemoglobins; D006657:Histones; D012709:Serum Albumin; D000255:Adenosine Triphosphate; D004247:DNA; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; C534281:CTSL protein, human; D056668:Cathepsin L