Literature summary for 3.4.24.34 extracted from

Aschi, M.; Besker, N.; Re, N.; Pochetti, G.; Coletti, C.; Gallina, C.; Mazza, F.
Stereoselectivity by enantiomeric inhibitors of matrix metalloproteinase-8: new insights from molecular dynamics simulations (2007), J. Med. Chem., 50, 211-218.

Search for more literature for 3.4.24.34

Inhibitors

Inhibitors	Comment	Organism	Structure
(R)-[1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl] phosphonate	stereoselectivity, binding structure, molecular dynamic simulations of inhibitor bound to MMP-8, the 144-155 loop of the enzyme undergoes a drastic decrease of mobility once complexed with the enantiomer, overview	Homo sapiens
(S)-[1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl] phosphonate	stereoselectivity, binding structure, molecular dynamic simulations of inhibitor bound to MMP-8, the 144-155 loop of the enzyme undergoes a drastic decrease of mobility once complexed with the enantiomer, overview	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Subunits

Subunits	Comment	Organism
More	molecular dynamic simulations of MMP-8 with and without bound inhibitor, the 144-155 loop of the enzyme undergoes a drastic decrease of mobility once complexed with both enantiomers, S1' subsite structure, overview	Homo sapiens

Synonyms

Synonyms	Comment	Organism
MMP-8	-	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)