scholarly journals Identification by nuclear magnetic resonance spectroscopy of an active-site hydrogen-bond network in human monoacylglycerol lipase (hMGL): implications for hMGL dynamics, pharmacological inhibition, and catalytic mechanism

2010 ◽  
Vol 6 (8) ◽  
pp. 1381 ◽  
Author(s):  
Ioannis Karageorgos ◽  
Sergiy Tyukhtenko ◽  
Nikolai Zvonok ◽  
David R. Janero ◽  
Christine Sallum ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Hydrogen Bond ◽  
Magnetic Resonance ◽  
Magnetic Resonance Spectroscopy ◽  
Active Site ◽  
Catalytic Mechanism ◽  
Resonance Spectroscopy ◽  
Monoacylglycerol Lipase ◽  
Hydrogen Bond Network ◽  
Bond Network

A hydrogen-bond network at the active site of subtilisin BPN'

1970 ◽  
Vol 257 (813) ◽  
pp. 119-124 ◽  
Keyword(s):  
Hydrogen Bond ◽  
Active Site ◽  
Serine Proteases ◽  
Catalytic Mechanism ◽  
Three Dimensional ◽  
Hydrogen Bond Network ◽  
The Common ◽  
Bond Network ◽  
The One ◽  
Active Site Region

Further examination of the active site region in our X-ray crystallographic model of subtilisin BPN' reveals a hydrogen-bond network that bears a remarkable resemblance to the one found in a- chymotrypsin. It involves the side chains of the reactive Ser-221, His-64, Asp-32 and Ser-33. Otherwise the two enzymes have entirely different three-dimensional structures. This observation suggests that the common hydrogen bond network plays some essential role in the catalytic mechanism of serine proteases generally.

Nuclear magnetic resonance studies of the interaction of inhibitors with chymotrypsin. N-Trifluoroacetyl derivatives of phenylalanine

1973 ◽  
Vol 26 (1) ◽  
pp. 135 ◽  
Author(s):  
BC Nicholson ◽  
TM Spotswood
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Chemical Shift ◽  
Magnetic Resonance Spectroscopy ◽  
Active Site ◽  
Molar Ratio ◽  
Resonance Spectroscopy ◽  
Magnetic Resonance Studies ◽  
Derivatives Of ◽  
Nuclear Magnetic

The binding of N-trifluoroacetyl derivatives of phenylalanine to the enzyme chymotrypsin has been studied by 19F nuclear magnetic resonance spectroscopy. Separate resonances are observed for the D- and L- enantiomers in the presence of chymotrypsin and their difference in chemical shift is dependent on the molar ratio of inhibitor to enzyme. The results are interpreted in terms of the known structure of the active site and possible modes of reorientation of the aromatic ring in its binding site. Approximate and accurate methods of quantifying the data are discussed and values for the dissociation constant (KI) of the EI complex, and the change in chemical shift on binding, are reported for the D-isomers.

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