Full activation of MMP1

Stable Identifier
Reaction [transition]
Homo sapiens
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The 42 kDa intermediate form of MMP1 is fully activated by cleavage of the Gln99-Phe100 bond, producing a 41 kDa protein. MMP2 (Crabbe et al. 1994), MMP3 (Suzuki et al. 1990, Nagase et al. 1992), MMP7 (Imai et al. 1995), MMP10 (Nicholson et al. 1989) and MMP11 (Murphy et al. 1993) are able to convert the 42 kDa intermediate to fully activated 41 kDa form though they are not able to initiate activation of proMMP1 effectively (Nagase et al. 1992). MMP3 regulates MMP1 collagenase activity in human rheumatoid synovial fibroblasts (Unemori et al. 1991).
Literature References
PubMed ID Title Journal Year
2169257 The role of matrix metalloproteinase 3 in the stepwise activation of human rheumatoid synovial procollagenase

Salvesen, G, Nagase, H, Ito, A, Suzuki, K, Enghild, JJ

Biol Chem Hoppe Seyler 1990
1480033 Activation mechanisms of the precursors of matrix metalloproteinases 1, 2 and 3

Morodomi, T, Salvesen, G, Nagase, H, Suzuki, K, Enghild, JJ

Matrix Suppl 1992
7981201 Reciprocated matrix metalloproteinase activation: a process performed by interstitial collagenase and progelatinase A

Smith, BJ, O'Connell, JP, Docherty, AJ, Crabbe, T

Biochemistry 1994
Catalyst Activity

serine-type endopeptidase activity of MMP2,3,7,10,11 [extracellular region]

Orthologous Events
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