Literature summary for 3.4.24.34 extracted from

Gioia, M.; Fasciglione, G.F.; Marini, S.; D'Alessio, S.; De Sanctis, G.; Diekmann, O.; Pieper, M.; Politi, V.; Tschesche, H.; Coletta, M.
Modulation of the catalytic activity of neutrophil collagenase MMP-8 on bovine collagen I. Role of the activation cleavage and of the hemopexin-like domain (2002), J. Biol. Chem., 277, 23123-23130.

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Cloned(Commentary)

Cloned (Comment)	Organism
recombinant catalytic domains displaying either Phe 79, PheMMP-8 or Met80, MetMMP-8	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
batimastat	BB-94, peptidomimetic MMP inhibitor	Homo sapiens

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0533	-	bovine collagen I	pH 7.4, 37°C	Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	Zn2+ metalloendopeptidase	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	human	-

Purification (Commentary)

Purification (Comment)	Organism
whMMP-8 proenzyme	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
bovine collagen I + H2O	-	Homo sapiens	?	-	?

Synonyms

Synonyms	Comment	Organism
MetMMP-8	-	Homo sapiens
MMP-8	-	Homo sapiens
neutrophil collagenase	-	Homo sapiens
PheMMP-8	-	Homo sapiens
whMMP-8	-	Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
4.75	-	bovine collagen I	pH 7.4, 37°C	Homo sapiens

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Release 2023.1 (January 2023)