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

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

Role of an evolutionarily invariant serine for the stability of human carbonic anhydrase II

1992 ◽  
Vol 1118 (2) ◽  
pp. 179-186 ◽  
Author(s):  
Lars Göran Mårtensson ◽  
Bengt-Harald Jonsson ◽  
Magdalena Andersson ◽  
Anne Kihlgren ◽  
Nils Bergenhem ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Ii ◽  
Human Carbonic Anhydrase ◽  
The Stability

scholarly journals Exploration of the residues modulating the catalytic features of human carbonic anhydrase XIII by a site-specific mutagenesis approach

2019 ◽  
Vol 34 (1) ◽  
pp. 1506-1510
Author(s):  
Giuseppina De Simone ◽  
Anna Di Fiore ◽  
Emanuela Truppo ◽  
Emma Langella ◽  
Daniela Vullo ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Site Specific ◽  
Human Carbonic Anhydrase ◽  
A Site

GroEL/ES-mediated refolding of human carbonic anhydrase II: role of N-terminal helices as recognition motifs for GroEL

1995 ◽  
Vol 1247 (2) ◽  
pp. 195-200 ◽  
Author(s):  
Malin Persson ◽  
Göran Aronsson ◽  
Nils Bergenhem ◽  
Per-Ola Freskgård ◽  
Bengt-Harald Jonsson ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Ii ◽  
Human Carbonic Anhydrase ◽  
Recognition Motifs
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