Results 171 to 180 of about 130,822 (183)

Identification of the carbonic anhydrase II binding site in the Cl(-)/HCO(3)(-) anion exchanger AE1.

Biochemistry, 2000
The human Cl(-)/HCO(3)(-) anion exchanger (AE1) possesses a binding site within its 33 residue carboxyl-terminal region (Ct) for carbonic anhydrase II (CAII). The amino acid sequence comprising this CAII binding site was determined by peptide competition
J. W. Vince, R. A. F. Reithmeier
semanticscholar   +1 more source

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

Biochemistry, 1989
To test the hypothesis that histidine 64 in the active site of human carbonic anhydrase II functions as a proton-transfer group in the catalysis of CO2 hydration, we have studied a site-specific mutant having histidine 64 replaced by alanine, which ...
C. Tu, D. Silverman, C. Forsman, B. Jonsson, S. Lindskog   +4 more
semanticscholar   +1 more source

A novel carbonic anhydrase II binding site regulates NHE1 activity.

Biochemistry, 2006
Carbonic anhydrase II (CAII) binds to and regulates transport by the NHE1 isoform of the mammalian Na(+)/H(+) exchanger. We localized and characterized the CAII binding region on the C-terminal tail of the Na(+)/H(+) exchanger.
Xiuju Li, Yongsheng Liu, B. Alvarez, J. Casey, L. Fliegel   +4 more
semanticscholar   +1 more source

Carbonic anhydrase II deficiency.

Bone, 2023
M. Whyte
semanticscholar   +1 more source

Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II.

Journal of Molecular Biology, 1996
Perdeuteration of all non-exchangeable proton sites can significantly increase the size of proteins and protein complexes for which NMR resonance assignments and structural studies are possible.
R. Venters, R. Venters, B. Farmer, B. Farmer, C. Fierke, C. Fierke, L. Spicer, L. Spicer   +7 more
semanticscholar   +1 more source

QM/MM calculations reveal the different nature of the interaction of two carborane-based sulfamide inhibitors of human carbonic anhydrase II.

Journal of Physical Chemistry B, 2013
The crystal structures of two novel carborane-sulfamide inhibitors in the complex with human carbonic anhydrase II (hCAII) have been studied using QM/MM calculations. Even though both complexes possess the strongly interacting sulfamide···zinc ion motif,
Adam Pecina, M. Lepšík, J. Řezáč, J. Brynda, P. Mader, P. Řezáčová, P. Hobza, J. Fanfrlík   +7 more
semanticscholar   +1 more source

New amino acid clubbed Schiff bases inhibit carbonic anhydrase II, α-glucosidase, and urease enzymes: in silico and in vitro

, 2021
Kashif Rafiq, Majid Khan, Niaz Muhammed, Ajmal Khan, Najeeb Ur Rehman, Balqees Essa Mohammad Al-Yahyaei, Mohammed Khiat, S. Halim, Zarbad Shah, R. Csuk, A. Al‐Harrasi   +10 more
semanticscholar   +1 more source

Localization of the Cl-/HCO3- anion exchanger binding site to the amino-terminal region of carbonic anhydrase II.

Biochemistry, 2000
Human carbonic anhydrase II (CAII) possesses a binding site for an acidic motif (D887ADD) within the carboxyl-terminal region (Ct) of the human erythrocyte chloride/bicarbonate anion exchanger, AE1.
J. W. Vince, U. Carlsson, R. Reithmeier
semanticscholar   +1 more source

Structure of bovine carbonic anhydrase II at 1.95 A resolution.

Acta Crystallographica Section D: Biological Crystallography, 2004
Carbonic anhydrase (CA) is a zinc-containing enzyme that catalyzes the reversible hydration of CO2 to HCO3-. In eukaryotes, the enzyme plays a role in various physiological functions, including interconversion between CO2 and HCO3- in intermediary ...
R. Saito, Takao Sato, A. Ikai, N. Tanaka
semanticscholar   +1 more source

Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: A pentacoordinated binding of the SCN− ion to the zinc at high pH

Proteins: Structure, Function, and Bioinformatics, 1990
The binding of four inhibitors—mercuric ion, 3‐acetoxymercuri‐4‐aminobenzenesulfonamide (AMS), acetazolamide (Diamox), and thiocyanate ion—to human carbonic anhydrase II (HCA II) has been studied with X‐ray crystallography.
A. Eriksson, P. Kylsten, T. Jones, A. Liljas   +3 more
semanticscholar   +1 more source