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 Site-directed mutagenesis of human carbonic anhydrase I: structure and function

1996 ◽  
Vol 52 (a1) ◽  
pp. C134-C134
Author(s):  
K. K. Kannan ◽  
A. K. Mohanty ◽  
M. V. Hosur ◽  
M. B. Satayamurty ◽  
A. V. S. S. Narayan Rao ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Structure And Function ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Carbonic Anhydrase I ◽  
Human Carbonic Anhydrase ◽  
And Function

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

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 Structural implications of the C-terminal tail in the catalytic and stability properties of manganese peroxidases from ligninolytic fungi

2014 ◽  
Vol 70 (12) ◽  
pp. 3253-3265 ◽  
Author(s):  
Elena Fernández-Fueyo ◽  
Sandra Acebes ◽  
Francisco J. Ruiz-Dueñas ◽  
María Jesús Martínez ◽  
Antonio Romero ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Electron Transfer ◽  
Manganese Peroxidase ◽  
Catalytic Properties ◽  
Substrate Oxidation ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Ceriporiopsis Subvermispora ◽  
Ligninolytic Fungi ◽  
Access Channel

The genome ofCeriporiopsis subvermisporaincludes 13 manganese peroxidase (MnP) genes representative of the three subfamilies described in ligninolytic fungi, which share an Mn2+-oxidation site and have varying lengths of the C-terminal tail. Short, long and extralong MnPs were heterologously expressed and biochemically characterized, and the first structure of an extralong MnP was solved. Its C-terminal tail surrounds the haem-propionate access channel, contributing to Mn2+oxidation by the internal propionate, but prevents the oxidation of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS), which is only oxidized by short MnPs and by shortened-tail variants from site-directed mutagenesis. The tail, which is anchored by numerous contacts, not only affects the catalytic properties of long/extralong MnPs but is also associated with their high acidic stability. Cd2+binds at the Mn2+-oxidation site and competitively inhibits oxidation of both Mn2+and ABTS. Moreover, mutations blocking the haem-propionate channel prevent substrate oxidation. This agrees with molecular simulations that position ABTS at an electron-transfer distance from the haem propionates of anin silicoshortened-tail form, while it cannot reach this position in the extralong MnP crystal structure. Only small differences exist between the long and the extralong MnPs, which do not justify their classification as two different subfamilies, but they significantly differ from the short MnPs, with the presence/absence of the C-terminal tail extension being implicated in these differences.

scholarly journals Tailoring a Soluble Diiron Monooxygenase for Synthesis of Aromatic N-oxides

Catalysts ◽  
2019 ◽  
Vol 9 (4) ◽  
pp. 356 ◽  
Author(s):  
Vytautas Petkevičius ◽  
Justas Vaitekūnas ◽  
Dovydas Vaitkus ◽  
Narimantas Čėnas ◽  
Rolandas Meškys
Keyword(s):  
Organic Chemistry ◽  
Escherichia Coli ◽  
Active Site ◽  
Catalytic Properties ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Wild Type ◽  
Work Site ◽  
Whole Cells ◽  
New Variant

The aromatic N-oxides have received increased attention over the last few years due to their potential application in medicine, agriculture and organic chemistry. As a green alternative in their synthesis, the biocatalytic method employing whole cells of Escherichia coli bearing phenol monooxygenase like protein PmlABCDEF (from here on – PML monooxygenase) has been introduced. In this work, site-directed mutagenesis was used to study the contributions of active site neighboring residues I106, A113, G109, F181, F200, F209 to the regiospecificity of N-oxidation. Based on chromogenic indole oxidation screening, a collection of PML mutants with altered catalytic properties was created. Among the tested mutants, the A113G variant acquired the most distinguishable N-oxidations capacity. This new variant of PML was able to produce dioxides (quinoxaline-1,4-dioxide, 2,5-dimethylpyrazine-1,4-dioxide) and specific mono-N-oxides (2,3,5-trimethylpyrazine-1-oxide) that were unachievable using the wild type PML. This mutant also featured reshaped regioselectivity as N-oxidation shifted towards quinazoline-1-oxide compared to quinazoline-3-oxide that is produced by the wild type PML.

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