X-ray snapshots of serine protease catalysis reveal a tetrahedral intermediate.
Studies on the catalytic mechanism and inhibition of serine proteases are widely used as paradigms for teaching enzyme catalysis. Ground-breaking work on the structures of chymotrypsin and subtilisin led to the idea of a conserved catalytic triad formed by the active site Ser, His and Asp residues....
Asıl Yazarlar: | Wilmouth, R, Edman, K, Neutze, R, Wright, P, Clifton, I, Schneider, T, Schofield, C, Hajdu, J |
---|---|
Materyal Türü: | Journal article |
Dil: | English |
Baskı/Yayın Bilgisi: |
2001
|
Benzer Materyaller
-
Structural analyses on intermediates in serine protease catalysis.
Yazar:: Liu, B, ve diğerleri
Baskı/Yayın Bilgisi: (2006) -
X-ray structure of a serine protease acyl-enzyme complex at 0.95-A resolution.
Yazar:: Katona, G, ve diğerleri
Baskı/Yayın Bilgisi: (2002) -
Molecular dynamics simulations of the acyl-enzyme and the tetrahedral intermediate in the deacylation step of serine proteases.
Yazar:: Topf, M, ve diğerleri
Baskı/Yayın Bilgisi: (2002) -
Mechanistic insights into the inhibition of serine proteases by monocyclic lactams.
Yazar:: Wilmouth, R, ve diğerleri
Baskı/Yayın Bilgisi: (1999) -
beta-Sultams - A novel class of serine protease inhibitors
Yazar:: Beardsell, M, ve diğerleri
Baskı/Yayın Bilgisi: (2001)