scholarly journals Tryptophan Synthase Uses an Atypical Mechanism To Achieve Substrate Specificity

Biochemistry ◽  
2016 ◽  
Vol 55 (51) ◽  
pp. 7043-7046 ◽  
Author(s):  
Andrew R. Buller ◽  
Paul van Roye ◽  
Javier Murciano-Calles ◽  
Frances H. Arnold
Keyword(s):  
Substrate Specificity ◽  
Tryptophan Synthase

βD305A Mutant of Tryptophan Synthase Shows Strongly Perturbed Allosteric Regulation and Substrate Specificity†

Biochemistry ◽  
2001 ◽  
Vol 40 (25) ◽  
pp. 7421-7432 ◽  
Author(s):  
Davide Ferrari ◽  
Li-Hong Yang ◽  
Edith W. Miles ◽  
Michael F. Dunn
Keyword(s):  
Substrate Specificity ◽  
Allosteric Regulation ◽  
Tryptophan Synthase

scholarly journals Functionalized Bilayer Membranes as Artificial Tryptophan Synthase. Characterization of Catalytic Efficiency, Substrate Specificity, and Reaction Selectivity

1990 ◽  
Vol 63 (8) ◽  
pp. 2339-2345 ◽  
Author(s):  
Yukito Murakami ◽  
Jun-ichi Kikuchi ◽  
Yoshio Hisaeda ◽  
Koichiro Nakamura ◽  
Tomoyuki Kitazaki ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Catalytic Efficiency ◽  
Tryptophan Synthase ◽  
Bilayer Membranes ◽  
Reaction Selectivity

scholarly journals DEFINING SUBSTRATE SPECIFICITY IN TRYPTOPHAN SYNTHASE BETA‐SUBUNIT HOMOLOGS

2007 ◽  
Vol 21 (6) ◽  
Author(s):  
Santiago Lima ◽  
Christopher Schlett ◽  
Michael W.W. Adams ◽  
Michael Kaufmann ◽  
Boris Striepen ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Beta Subunit ◽  
Tryptophan Synthase

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
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