scholarly journals Functional role of a putative carbonic anhydrase II-binding domain in the electrogenic Na+-HCO3−cotransporter NBCe1 expressed in Xenopus oocytes

Channels ◽  
2011 ◽  
Vol 5 (2) ◽  
pp. 106-109 ◽  
Author(s):  
Hideomi Yamada ◽  
Shoko Horita ◽  
Masashi Suzuki ◽  
Toshiro Fujita ◽  
George Seki
Keyword(s):  
Carbonic Anhydrase ◽  
Functional Role ◽  
Xenopus Oocytes ◽  
Binding Domain ◽  
Carbonic Anhydrase Ii

scholarly journals Structure and Functional Role of Dynein's Microtubule-Binding Domain

Science ◽  
2008 ◽  
Vol 322 (5908) ◽  
pp. 1691-1695 ◽  
Author(s):  
A. P. Carter ◽  
J. E. Garbarino ◽  
E. M. Wilson-Kubalek ◽  
W. E. Shipley ◽  
C. Cho ◽  
...  
Keyword(s):  
Functional Role ◽  
Binding Domain ◽  
Microtubule Binding ◽  
Microtubule Binding Domain

scholarly journals Identification and functional role of the carbonic anhydrase Cah3 in thylakoid membranes of pyrenoid of Chlamydomonas reinhardtii

2012 ◽  
Vol 1817 (8) ◽  
pp. 1248-1255 ◽  
Author(s):  
Maria A. Sinetova ◽  
Elena V. Kupriyanova ◽  
Alexandra G. Markelova ◽  
Suleyman I. Allakhverdiev ◽  
Natalia A. Pronina
Keyword(s):  
Carbonic Anhydrase ◽  
Chlamydomonas Reinhardtii ◽  
Functional Role ◽  
Thylakoid Membranes

scholarly journals Structural insights into the functional role of the Hcn sub-domain of the receptor-binding domain of the botulinum neurotoxin mosaic serotype C/D

Biochimie ◽  
2013 ◽  
Vol 95 (7) ◽  
pp. 1379-1385 ◽  
Author(s):  
Yanfeng Zhang ◽  
Anna S. Gardberg ◽  
Thomas E. Edwards ◽  
Banumathi Sankaran ◽  
Howard Robinson ◽  
...  
Keyword(s):  
Receptor Binding ◽  
Functional Role ◽  
Botulinum Neurotoxin ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Structural Insights

Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant

Biochemistry ◽  
1989 ◽  
Vol 28 (19) ◽  
pp. 7913-7918 ◽  
Author(s):  
Chingkuang Tu ◽  
David N. Silverman ◽  
Cecilia Forsman ◽  
Bengt Harald Jonsson ◽  
Sven Lindskog
Keyword(s):  
Carbonic Anhydrase ◽  
Catalytic Mechanism ◽  
Carbonic Anhydrase Ii ◽  
Site Specific ◽  
Human Carbonic Anhydrase ◽  
A Site

The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase

1999 ◽  
Vol 261 (2) ◽  
pp. 379-391 ◽  
Author(s):  
Susanne Dopner ◽  
Peter Hildebrandt ◽  
Federico I. Rosell ◽  
A. Grant Mauk ◽  
Matthias von Walter ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Functional Role ◽  
Binding Domain ◽  
Lysine Residues

scholarly journals Role of Hydrophilic Residues in Proton Transfer during Catalysis by Human Carbonic Anhydrase II†‡

Biochemistry ◽  
2008 ◽  
Vol 47 (46) ◽  
pp. 12028-12036 ◽  
Author(s):  
Jiayin Zheng ◽  
Balendu Sankara Avvaru ◽  
Chingkuang Tu ◽  
Robert McKenna ◽  
David N. Silverman
Keyword(s):  
Carbonic Anhydrase ◽  
Proton Transfer ◽  
Carbonic Anhydrase Ii ◽  
Human Carbonic Anhydrase ◽  
Hydrophilic Residues

scholarly journals Importance of C-Terminal Knot Structure in Carbonic Anhydrase II (Part I): Role of C-Terminal Knot Forming GLN253 on Enzymatic Property of Human Carbinic II

1970 ◽  
Vol 14 ◽  
pp. 1-9
Author(s):  
Mohammad Taufiq Alam
Keyword(s):  
Amino Acid ◽  
Carbonic Anhydrase ◽  
Point Mutation ◽  
Amino Acid Residue ◽  
Active Site ◽  
Terminal Region ◽  
Carbonic Anhydrase Ii ◽  
C Terminus ◽  
Human Carbonic Anhydrase

In both, bovine and human carbonic anhydrase II, a conserved glutamine residue occupies the position in the middle of the knot, which is formed by intercrossing of C-terminal end with N-terminal region. Previous studies have indicated that C-terminus is not the part of an active site, but truncation of 7 amino acid residue in this region can have marked effects on stability of the enzyme (data not published). To gain further insight into the role of specific amino acid residue in C-terminal region, site directed mutagenesis was used to introduce point mutation. Substitution of glutamine with cysteine was chosen because the cysteine residue is less hydrophilic as compared with glutamine and thus, may disrupt the hydrophilic environment in this region. Result indicates that Gln253 located within the C-terminus knot topology plays a significant role in normal function of the enzyme. Thus, C-terminal region might mediate cooperativity between the central active site of the enzyme through proper formation of knot. Key words: Human carbonic anhydrase II; knot topology; point mutation J. bio-sci. 14: 1-9, 2006

scholarly journals The Human Carbonic Anhydrase II in Platelets: An Underestimated Field of Its Activity

2018 ◽  
Vol 2018 ◽  
pp. 1-10 ◽  
Author(s):  
Maciej Jakubowski ◽  
Ewa Szahidewicz-Krupska ◽  
Adrian Doroszko
Keyword(s):  
Carbonic Anhydrase ◽  
Current Knowledge ◽  
Short Review ◽  
Carbonic Anhydrase Ii ◽  
Carbonic Anhydrases ◽  
Direct Role ◽  
Novel Strategy ◽  
The Impact ◽  
First Time

Carbonic anhydrases constitute a group of enzymes that catalyse reversible hydration of carbon dioxide leading to the formation of bicarbonate and proton. The platelet carbonic anhydrase II (CAII) was described for the first time in the '80s of the last century. Nevertheless, its direct role in platelet physiology and pathology still remains poorly understood. The modulation of platelet CAII action as a therapeutic approach holds promise as a novel strategy to reduce the impact of cardiovascular diseases. This short review paper summarises the current knowledge regarding the role of human CAII in regulating platelet function. The potential future directions considering this enzyme as a potential drug target and important pathophysiological chain in platelet-related disorders are described.

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