Catalytic Function of a Vital Carboxylate Residue in the Beta Subunit of the CF1-Atpase from C. Reinhardtii

1995 ◽  
pp. 2071-2074
Author(s):  
C.-Y. Hu ◽  
A. L. P. Houseman ◽  
L. Morgan ◽  
A. N. Webber ◽  
W. D. Frasch
Keyword(s):  
Beta Subunit ◽  
Catalytic Function

scholarly journals A beta subunit mutation disrupting the catalytic function of Escherichia coli RNA polymerase.

1991 ◽  
Vol 88 (14) ◽  
pp. 6018-6022 ◽  
Author(s):  
J. Lee ◽  
M. Kashlev ◽  
S. Borukhov ◽  
A. Goldfarb
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Beta Subunit ◽  
Catalytic Function

63 SAP-97 promotes hKv1.5 compartmentation to lipid rafts and interaction with beta-subunit: consequences on currents properties

2003 ◽  
Vol 2 (1) ◽  
pp. 4
Author(s):  
A MAGUY ◽  
D GODREAU ◽  
P RATAJCZAK ◽  
C HEYMES ◽  
R VRANCKX ◽  
...  
Keyword(s):  
Lipid Rafts ◽  
Beta Subunit

Human Chorionic Gonadotropin and CA 15-3 Producing Adenocarcinoma

1998 ◽  
Vol 37 (08) ◽  
pp. 297-298 ◽  
Author(s):  
A. Özet ◽  
A. Arpaci ◽  
S. Kömiircü ◽  
G. Üçkaya
Keyword(s):  
Lung Adenocarcinoma ◽  
Chorionic Gonadotropin ◽  
Human Chorionic Gonadotropin ◽  
Carbohydrate Antigen ◽  
Beta Subunit ◽  
Cancer Antigen ◽  
First Report ◽  
Primary Lung Adenocarcinoma ◽  
Adenocarcinoma Of Lung

Summary50 years old man suffering from primary lung adenocarcinoma presented with high levels of both beta subunit human chorionic gonadotropin (βHCG) and cancer antigen 15-3 (CA 15-3) in the absence of elevated carcinoembrionic antigen (CEA), alfa fetoprotein (AFP) and carbohydrate antigen 19-9 (CA 19-9). Although βHCG or CA 15-3 high levels were reported in adenocarcinoma of lung, this is the first report of a patient with high levels of both markers.

Biochemical study of fibrinolytic protease from Euphausia superba possessing multifunctional serine protease activity

2020 ◽  
Vol 27 ◽  
Author(s):  
Guo-Ying Qian ◽  
Gyutae Lim ◽  
Shang-Jun Yin ◽  
Jun-Mo Yang ◽  
Jinhyuk Lee ◽  
...  
Keyword(s):  
Defense Mechanisms ◽  
Fluorescence Spectra ◽  
Biochemical Study ◽  
Euphausia Superba ◽  
Md Simulations ◽  
Time Interval ◽  
Serine Residue ◽  
Catalytic Function ◽  
Serine Protease Activity ◽  
Key Residues

Background: Background: Fibrinolytic protease from Euphausia superba (EFP) was isolated. Objective: Biochemical distinctions, regulation of the catalytic function, and the key residues of EFP were investigated. Methods: The serial inhibition kinetic evaluations coupled with measurements of fluorescence spectra in the presence of 4- (2-aminoethyl) benzene sulfonyl fluoride hydrochloride (AEBSF) was conducted. The computational molecular dynamics (MD) simulations were also applied for a comparative study. Results: The enzyme behaved as a monomeric protein with a molecular mass of about 28.6 kD with Km BApNA = 0.629 ± 0.02 mM and kcat/Km BApNA = 7.08 s-1 /mM. The real-time interval measurements revealed that the inactivation was a first-order reaction, with the kinetic processes shifting from a monophase to a biphase. Measurements of fluorescence spectra showed that serine residue modification by AEBSF directly caused conspicuous changes of the tertiary structures and exposed hydrophobic surfaces. Some osmolytes were applied to find protective roles. These results confirmed that the active region of EFP is more flexible than the overall enzyme molecule and serine, as the key residue, is associated with the regional unfolding of EFP in addition to its catalytic role. The MD simulations were supportive to the kinetics data. Conclusion: Our study indicated that EFP has an essential serine residue for its catalyst function and associated folding behaviors. Also, the functional role of osmolytes such as proline and glycine that may play a role in defense mechanisms from environmental adaptation in a krill’s body was suggested.

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