Influence of amino acid replacement at position 198 on catalytic properties of zinc-bound water in human carbonic anhydrase III

Biochemistry ◽  
1993 ◽  
Vol 32 (22) ◽  
pp. 5786-5791 ◽  
Author(s):  
Philip V. LoGrasso ◽  
Chingkuang Tu ◽  
Xian Chen ◽  
Shinichi Taoka ◽  
Philip J. Laipis ◽  
...  
Keyword(s):  
Amino Acid ◽  
Carbonic Anhydrase ◽  
Catalytic Properties ◽  
Bound Water ◽  
Amino Acid Replacement ◽  
Carbonic Anhydrase Iii ◽  
Human Carbonic Anhydrase

Enhancement of the catalytic properties of human carbonic anhydrase III by site-directed mutagenesis

Biochemistry ◽  
1991 ◽  
Vol 30 (6) ◽  
pp. 1484-1490 ◽  
Author(s):  
David A. Jewell ◽  
Chingkuang Tu ◽  
Shanthi R. Paranawithana ◽  
Susan M. Tanhauser ◽  
Philip V. LoGrasso ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Catalytic Properties ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Carbonic Anhydrase Iii ◽  
Human Carbonic Anhydrase

scholarly journals Synthesis and human carbonic anhydrase I, II, VA, and XII inhibition with novel amino acid–sulphonamide conjugates

2020 ◽  
Vol 35 (1) ◽  
pp. 489-497 ◽  
Author(s):  
Hasan Küçükbay ◽  
Nesrin Buğday ◽  
F. Zehra Küçükbay ◽  
Andrea Ageli ◽  
Gianluca Bartolucci ◽  
...  
Keyword(s):  
Amino Acid ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase

Interaction and influence of phenylalanine-198 and threonine-199 on catalysis by human carbonic anhydrase III

Biochemistry ◽  
1993 ◽  
Vol 32 (31) ◽  
pp. 7861-7865 ◽  
Author(s):  
Xian Chen ◽  
Chingkuang Tu ◽  
Philip V. LoGrasso ◽  
Philip J. Laipis ◽  
David N. Silverman
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Iii ◽  
Human Carbonic Anhydrase

Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III

2007 ◽  
Vol 68 (1) ◽  
pp. 337-343 ◽  
Author(s):  
Ileana Elder ◽  
Zoë Fisher ◽  
Philip J. Laipis ◽  
Chingkuang Tu ◽  
Robert McKenna ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Kinetic Analysis ◽  
Active Site ◽  
Carbonic Anhydrase Iii ◽  
Human Carbonic Anhydrase

Characterization of human carbonic anhydrase III from skeletal muscle

1979 ◽  
Vol 17 (9-10) ◽  
pp. 837-854 ◽  
Author(s):  
Nicholas Carter ◽  
Stephen Jeffery ◽  
Alan Shiels ◽  
Yvonne Edwards ◽  
Terry Tipler ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Iii ◽  
Human Carbonic Anhydrase

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 deduced amino acid sequence of human carbonic anhydrase-related protein (CARP) is 98% identical to the mouse homologue

Gene ◽  
1993 ◽  
Vol 126 (2) ◽  
pp. 291-292 ◽  
Author(s):  
Laura A. Skaggs ◽  
Nils C.H. Bergenhem ◽  
Patrick J. Venta ◽  
Richard E. Tashian
Keyword(s):  
Amino Acid ◽  
Carbonic Anhydrase ◽  
Amino Acid Sequence ◽  
Related Protein ◽  
Mouse Homologue ◽  
Human Carbonic Anhydrase
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