3.4.24.14: procollagen N-endopeptidase
This is an abbreviated version!
For detailed information about procollagen N-endopeptidase, go to the full flat file.
Word Map on EC 3.4.24.14
Reaction
Cleaves the N-propeptide of collagen chain alpha1(I) at Pro-/-Gln and of alpha1(II) and alpha2(I) at Ala-/-Gln
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Synonyms
ADAM-TS2, ADAMTS 3, ADAMTS proteinase, ADAMTS-2, ADAMTS14, ADAMTS2, ADAMTS3, aminoprocollagen endopeptidase, aminoprocollagen peptidase, aminoterminal procollagen peptidase, PC I-NP, pNPI, procollagen ADAMTS, procollagen aminopeptidase, procollagen aminoterminal protease, Procollagen I N-proteinase, Procollagen I/II amino-propeptide processing enzyme, procollagen I/II N-endopeptidase, procollagen III N-endopeptidase, procollagen III N-proteinase, Procollagen N-endopeptidase, procollagen N-protease, procollagen N-proteinase, procollagen N-terminal peptidase, procollagen N-terminal proteinase, Procollagen peptidase, type I/II procollagen N-proteinase
ECTree
Subunits
Subunits on EC 3.4.24.14 - procollagen N-endopeptidase
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monomer
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1* 107000, SDS-PAGE
additional information
further to proteolytic processing, the domain composition of ADAMTS2 can also result from an alternative splicing mechanism. Beside the classical 1211 amino acid full length enzyme, a shorter form has been described. It is formed by the first 543 amino acids of the long form (corresponding to exons 1-10) followed by 23 amino acids encoded by an alternative exon present in intron 10 of the long form. This truncated form does contain the metalloproteinase domain but does not show any significant aminoprocollagen peptidase activity
additional information
further to proteolytic processing, the domain composition of ADAMTS2 can also result from an alternative splicing mechanism. Beside the classical 1211 amino acid full length enzyme, a shorter form has been described. It is formed by the first 543 amino acids of the long form (corresponding to exons 1-10) followed by 23 amino acids encoded by an alternative exon present in intron 10 of the long form. This truncated form does contain the metalloproteinase domain but does not show any significant aminoprocollagen peptidase activity
additional information
further to proteolytic processing, the domain composition of ADAMTS2 can also result from an alternative splicing mechanism. Beside the classical 1211 amino acid full length enzyme, a shorter form has been described. It is formed by the first 543 amino acids of the long form (corresponding to exons 1-10) followed by 23 amino acids encoded by an alternative exon present in intron 10 of the long form. This truncated form does contain the metalloproteinase domain but does not show any significant aminoprocollagen peptidase activity
additional information
further to proteolytic processing, the domain composition of ADAMTS2 can also result from an alternative splicing mechanism. Beside the classical 1211 amino acid full length enzyme, a shorter form has been described. It is formed by the first 543 amino acids of the long form (corresponding to exons 1-10) followed by 23 amino acids encoded by an alternative exon present in intron 10 of the long form. This truncated form does contain the metalloproteinase domain but does not show any significant aminoprocollagen peptidase activity