Role of Second Coordination Sphere Amino Acid Residues on the Proton Transfer Mechanism of Human Carbonic Anhydrase II (HCA II)

2010 ◽  
Vol 114 (30) ◽  
pp. 7952-7959 ◽  
Author(s):  
V. Hakkim ◽  
V. Subramanian
Keyword(s):  
Amino Acid ◽  
Carbonic Anhydrase ◽  
Proton Transfer ◽  
Coordination Sphere ◽  
Transfer Mechanism ◽  
Carbonic Anhydrase Ii ◽  
Amino Acid Residues ◽  
Human Carbonic Anhydrase ◽  
Second Coordination Sphere

scholarly journals Effect of Active-site Mutation at Asn67 on the Proton Transfer Mechanism of Human Carbonic Anhydrase II

Biochemistry ◽  
2009 ◽  
Vol 48 (33) ◽  
pp. 7996-8005 ◽  
Author(s):  
C. Mark Maupin ◽  
Jiayin Zheng ◽  
Chingkuang Tu ◽  
Robert McKenna ◽  
David N. Silverman ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Proton Transfer ◽  
Active Site ◽  
Transfer Mechanism ◽  
Carbonic Anhydrase Ii ◽  
Site Mutation ◽  
Human Carbonic Anhydrase

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 Amino Acid Residues for Dioxygen Activation in the Second Coordination Sphere of the Dicopper Site of pMMO

2019 ◽  
Vol 58 (18) ◽  
pp. 12280-12288 ◽  
Author(s):  
Mayuko Miyanishi ◽  
Tsukasa Abe ◽  
Yuta Hori ◽  
Yoshihito Shiota ◽  
Kazunari Yoshizawa
Keyword(s):  
Amino Acid ◽  
Coordination Sphere ◽  
Dioxygen Activation ◽  
Amino Acid Residues ◽  
Second Coordination Sphere

Atomic Crystal and Molecular Dynamics Simulation Structures of Human Carbonic Anhydrase II:  Insights into the Proton Transfer Mechanism†,‡

Biochemistry ◽  
2007 ◽  
Vol 46 (11) ◽  
pp. 2930-2937 ◽  
Author(s):  
S. Zoë Fisher ◽  
C. Mark Maupin ◽  
Monika Budayova-Spano ◽  
Lakshmanan Govindasamy ◽  
Chingkuang Tu ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Carbonic Anhydrase ◽  
Proton Transfer ◽  
Transfer Mechanism ◽  
Dynamics Simulation ◽  
Carbonic Anhydrase Ii ◽  
Human Carbonic Anhydrase ◽  
Atomic Crystal

scholarly journals Water Networks in Fast Proton Transfer during Catalysis by Human Carbonic Anhydrase II

Biochemistry ◽  
2012 ◽  
Vol 52 (1) ◽  
pp. 125-131 ◽  
Author(s):  
Rose Mikulski ◽  
Dayne West ◽  
Katherine H. Sippel ◽  
Balendu Sankara Avvaru ◽  
Mayank Aggarwal ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Proton Transfer ◽  
Carbonic Anhydrase Ii ◽  
Water Networks ◽  
Fast Proton ◽  
Human Carbonic Anhydrase

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
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