Substrate and inhibitor specificity of kynurenine monooxygenase from Cytophaga hutchinsonii

2017 ◽  
Vol 27 (8) ◽  
pp. 1705-1708 ◽  
Author(s):  
Robert S. Phillips ◽  
Andrew D. Anderson ◽  
Harvey G. Gentry ◽  
Osman F. Güner ◽  
J. Phillip Bowen
Keyword(s):  
Inhibitor Specificity ◽  
Cytophaga Hutchinsonii

scholarly journals Fungal Cellulases VI. SUBSTRATE AND INHIBITOR SPECIFICITY OF THE fl-GLUCOSIDASE OF ST ACHYBOTRYS ATRA

1955 ◽  
Vol 8 (4) ◽  
pp. 577 ◽  
Author(s):  
MA Jermyn
Keyword(s):  
Marked Decrease ◽  
Inhibitor Specificity ◽  
Hydrolysis Of

A large number of compounds with glycosidic linkages have been tested as substrates for the ,8-glucosidase of Stachybotrys atm. The enzyme appears to be specific for ,8-glucosides and all configurational alterations to the D-glucopyranose ring or substitutions in it lead to non-substrates; phenyl-fl-thioglucoside is a substrate, however. Aryl-,8-glucosides have a higher affinity for the enzyme than alkyl-,8-glucosides and no hydrolysis of cellobiose by the enzyme can be demonstrated. arrha-Substitution in aryl-fl-glucosides leads to a marked decrease in the affinity between enzyme and substrate.

scholarly journals Adenosine kinase from rabbit liver. II. Substrate and inhibitor specificity

1979 ◽  
Vol 254 (7) ◽  
pp. 2346-2352 ◽  
Author(s):  
R.L. Miller ◽  
D.L. Adamczyk ◽  
W.H. Miller ◽  
G.W. Koszalka ◽  
J.L. Rideout ◽  
...  
Keyword(s):  
Adenosine Kinase ◽  
Rabbit Liver ◽  
Inhibitor Specificity

Abstract 1398: Impact of proteasome inhibitor specificity and efficacy on apoptosis induction by combination with ABT-199

2021 ◽  
Author(s):  
Sandra Weller ◽  
Benjamin Schaefer ◽  
Tobias Beigl ◽  
Kathrin Böpple ◽  
Walter E. Aulitzky ◽  
...  
Keyword(s):  
Proteasome Inhibitor ◽  
Apoptosis Induction ◽  
Inhibitor Specificity

scholarly journals The YRD Motif Is a Major Determinant of Substrate and Inhibitor Specificity in T-cell Protein-tyrosine Phosphatase

2001 ◽  
Vol 276 (28) ◽  
pp. 26036-26043 ◽  
Author(s):  
Ernest Asante-Appiah ◽  
Kristen Ball ◽  
Kevin Bateman ◽  
Kathryn Skorey ◽  
Rick Friesen ◽  
...  
Keyword(s):  
T Cell ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Major Determinant ◽  
Cell Protein ◽  
Inhibitor Specificity ◽  
Protein Tyrosine ◽  
The Yrd

Molecular Basis for p38 Protein Kinase Inhibitor Specificity

Biochemistry ◽  
1998 ◽  
Vol 37 (47) ◽  
pp. 16573-16581 ◽  
Author(s):  
JeanMarie Lisnock ◽  
Andy Tebben ◽  
Betsy Frantz ◽  
Edward A. O'Neill ◽  
Gist Croft ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Molecular Basis ◽  
Kinase Inhibitor ◽  
Protein Kinase Inhibitor ◽  
Inhibitor Specificity

scholarly journals A Disulfide Oxidoreductase (CHU_1165) Is Essential for Cellulose Degradation by Affecting Outer Membrane Proteins in Cytophaga hutchinsonii

2020 ◽  
Vol 86 (8) ◽  
Author(s):  
Dong Zhao ◽  
Ying Wang ◽  
Sen Wang ◽  
Weican Zhang ◽  
Qingsheng Qi ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Disulfide Bond ◽  
Cellulose Degradation ◽  
Outer Membrane Proteins ◽  
Hypothetical Protein ◽  
Pleiotropic Effect ◽  
Content Type ◽  
Cytophaga Hutchinsonii ◽  
Disulfide Oxidoreductase

ABSTRACT Cytophaga hutchinsonii cells can bind to the surface of insoluble cellulose and degrade it by utilizing a novel cell contact-dependent mechanism, in which the outer membrane proteins may play important roles. In this study, the deletion of a gene locus, chu_1165, which encodes a hypothetical protein with 32% identity with TlpB, a disulfide oxidoreductase in Flavobacterium psychrophilum, caused a complete cellulolytic defect in C. hutchinsonii. Further study showed that cells of the Δ1165 strain could not bind to cellulose, and the levels of many outer membrane proteins that can bind to cellulose were significantly decreased. The N-terminal region of CHU_1165 is anchored to the cytoplasmic membrane with five predicted transmembrane helices, and the C-terminal region is predicted to stretch to the periplasm and has a similar thioredoxin (Trx) fold containing a Cys-X-X-Cys motif that is conserved in disulfide oxidoreductases. Recombinant CHU_1165His containing the Cys-X-X-Cys motif was able to reduce the disulfide bonds of insulin in vitro. Site-directed mutation showed that the cysteines in the Cys-X-X-Cys motif and at residues 106 and 108 were indispensable for the function of CHU_1165. Western blotting showed that CHU_1165 was in an oxidized state in vivo, suggesting that it may act as an oxidase to catalyze disulfide bond formation. However, many of the decreased outer membrane proteins that were essential for cellulose degradation contained no or one cysteine, and mutation of the cysteine in these proteins did not affect cellulose degradation, indicating that CHU_1165 may have an indirect or pleiotropic effect on the function of these outer membrane proteins. IMPORTANCE Cytophaga hutchinsonii can rapidly digest cellulose in a contact-dependent manner, in which the outer membrane proteins may play important roles. In this study, a hypothetical protein, CHU_1165, characterized as a disulfide oxidoreductase, is essential for cellulose degradation by affecting the cellulose binding ability of many outer membrane proteins in C. hutchinsonii. Disulfide oxidoreductases are involved in disulfide bond formation. However, our studies show that many of the decreased outer membrane proteins that were essential for cellulose degradation contained no or one cysteine, and mutation of cysteine did not affect their function, indicating that CHU_1165 did not facilitate the formation of a disulfide bond in these proteins. It may have an indirect or pleiotropic effect on the function of these outer membrane proteins. Our study provides an orientation for exploring the proteins that assist in the appropriate conformation of many outer membrane proteins essential for cellulose degradation, which is important for exploring the novel mechanism of cellulose degradation in C. hutchinsonii.

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