Substrate specificity analysis and inhibitor design of homoisocitrate dehydrogenase

2007 ◽  
Vol 15 (3) ◽  
pp. 1346-1355 ◽  
Author(s):  
Takashi Yamamoto ◽  
Kentaro Miyazaki ◽  
Tadashi Eguchi
Keyword(s):  
Substrate Specificity ◽  
Inhibitor Design

scholarly journals DXP Synthase-Catalyzed CN Bond Formation: Nitroso Substrate Specificity Studies Guide Selective Inhibitor Design

ChemBioChem ◽  
2013 ◽  
Vol 14 (11) ◽  
pp. 1309-1315 ◽  
Author(s):  
Francine Morris ◽  
Ryan Vierling ◽  
Lauren Boucher ◽  
Jürgen Bosch ◽  
Caren L. Freel Meyers
Keyword(s):  
Substrate Specificity ◽  
Bond Formation ◽  
Selective Inhibitor ◽  
Inhibitor Design ◽  
Dxp Synthase

Mechanism-based isocoumarin inhibitors for serine proteases: Use of active site structure and substrate specificity in inhibitor design

1989 ◽  
Vol 39 (1) ◽  
pp. 33-46 ◽  
Author(s):  
James C. Powers ◽  
Chih-Min Kam ◽  
Lakshmi Narasimhan ◽  
Joszef Oleksyszyn ◽  
Maria A. Hernandez ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Active Site ◽  
Serine Proteases ◽  
Inhibitor Design ◽  
Site Structure ◽  
Active Site Structure

scholarly journals Using Substrate Specificity of Antiplasmin-Cleaving Enzyme for Fibroblast Activation Protein Inhibitor Design

Biochemistry ◽  
2009 ◽  
Vol 48 (23) ◽  
pp. 5149-5158 ◽  
Author(s):  
Kyung N. Lee ◽  
Kenneth W. Jackson ◽  
Simon Terzyan ◽  
Victoria J. Christiansen ◽  
Patrick A. McKee
Keyword(s):  
Substrate Specificity ◽  
Fibroblast Activation Protein ◽  
Protein Inhibitor ◽  
Inhibitor Design ◽  
Fibroblast Activation

Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity

2003 ◽  
Vol 70 ◽  
pp. 39-52 ◽  
Author(s):  
Roy A. Black ◽  
John R. Doedens ◽  
Rajeev Mahimkar ◽  
Richard Johnson ◽  
Lin Guo ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Recent Work ◽  
Tumour Necrosis Factor ◽  
Tumour Necrosis ◽  
Transforming Growth Factor ◽  
Intrinsic Activity ◽  
Converting Enzyme ◽  
Tumour Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor

Tumour necrosis factor α (TNFα)-converting enzyme (TACE/ADAM-17, where ADAM stands for a disintegrin and metalloproteinase) releases from the cell surface the extracellular domains of TNF and several other proteins. Previous studies have found that, while purified TACE preferentially cleaves peptides representing the processing sites in TNF and transforming growth factor α, the cellular enzyme nonetheless also sheds proteins with divergent cleavage sites very efficiently. More recent work, identifying the cleavage site in the p75 TNF receptor, quantifying the susceptibility of additional peptides to cleavage by TACE and identifying additional protein substrates, underlines the complexity of TACE-substrate interactions. In addition to substrate specificity, the mechanism underlying the increased rate of shedding caused by agents that activate cells remains poorly understood. Recent work in this area, utilizing a peptide substrate as a probe for cellular TACE activity, indicates that the intrinsic activity of the enzyme is somehow increased.

Substrate Specificity of Leukocyte and Platelet Elastases

1978 ◽  
Vol 39 (03) ◽  
pp. 785-786 ◽  
Author(s):  
Y Legrand ◽  
J Caen ◽  
L Robert
Keyword(s):  
Substrate Specificity

PRKACA mutations in adrenal Cushing can alter substrate specificity

2017 ◽  
Author(s):  
Kerstin Bathon ◽  
Isabel Weigand ◽  
Jens T Vanselow ◽  
Cristina L Ronchi ◽  
Dalmazi Guido Di ◽  
...  
Keyword(s):  
Substrate Specificity
Sign in / Sign up

Export Citation Format

Share Document