scholarly journals Bacillus pumilus Cyanide Dihydratase Mutants with Higher Catalytic Activity

2016 ◽  
Vol 7 ◽  
Author(s):  
Mary A. Crum ◽  
B. Trevor Sewell ◽  
Michael J. Benedik
Keyword(s):  
Catalytic Activity ◽  
Bacillus Pumilus ◽  
Cyanide Dihydratase

Increasing the catalytic activity of Bilirubin oxidase from Bacillus pumilus: Importance of host strain and chaperones proteins

2016 ◽  
Vol 230 ◽  
pp. 19-25 ◽  
Author(s):  
Sébastien Gounel ◽  
Jad Rouhana ◽  
Claire Stines-Chaumeil ◽  
Marine Cadet ◽  
Nicolas Mano
Keyword(s):  
Catalytic Activity ◽  
Bacillus Pumilus ◽  
Host Strain ◽  
Bilirubin Oxidase

scholarly journals Isolation and characterization of a cyanide dihydratase from Bacillus pumilus C1.

1993 ◽  
Vol 175 (19) ◽  
pp. 6105-6112 ◽  
Author(s):  
P R Meyers ◽  
D E Rawlings ◽  
D R Woods ◽  
G G Lindsey
Keyword(s):  
Bacillus Pumilus ◽  
Isolation And Characterization ◽  
Cyanide Dihydratase

scholarly journals CynD, the Cyanide Dihydratase from Bacillus pumilus: Gene Cloning and Structural Studies

2003 ◽  
Vol 69 (8) ◽  
pp. 4794-4805 ◽  
Author(s):  
Dakshina Jandhyala ◽  
Mark Berman ◽  
Paul R. Meyers ◽  
B. Trevor Sewell ◽  
Richard C. Willson ◽  
...  
Keyword(s):  
Bacillus Pumilus ◽  
Spiral Structure ◽  
Sequence Similarity ◽  
Affinity Purification ◽  
Three Dimensional ◽  
Pseudomonas Stutzeri ◽  
Recombinant Enzyme ◽  
Dimensional Reconstruction ◽  
Short Spiral ◽  
Cyanide Dihydratase

ABSTRACT The cyanide dihydratase in Bacillus pumilus was shown to be an 18-subunit spiral structure by three-dimensional reconstruction of electron micrographs of negatively stained material at its optimum pH, 8.0. At pH 5.4, the subunits rearrange to form an extended left-handed helix. Gel electrophoresis of glutaraldehyde cross-linked enzyme suggests that the fundamental component of the spiral is a dimer of the 37-kDa subunit. The gene was cloned, and the recombinant enzyme was readily expressed at high levels in Escherichia coli. Purification of the recombinant enzyme was facilitated by the addition of a C-terminal six-histidine affinity purification tag. The tagged recombinant enzyme has Km and V max values similar to those published for the native enzyme. This is the first cyanide dihydratase from a gram-positive bacterium to be sequenced, and it is the first description of the structure of any member of this enzyme class. The putative amino acid sequence shares over 80% identity to the only other sequenced cyanide dihydratase, that of the gram-negative Pseudomonas stutzeri strain AK61, and is similar to a number of other bacterial and fungal nitrilases. This sequence similarity suggests that the novel short spiral structure may be typical of these enzymes. In addition, an active cyanide dihydratase from a non-cyanide-degrading isolate of B. pumilus (strain 8A3) was cloned and expressed. This suggests that cynD, the gene coding for the cyanide dihydratase, is not unique to the C1 strain of B. pumilus and is not a reflection of its origin at a mining waste site.

scholarly journals The structure of the cyanide dihydratase (CynD) from Bacillus pumilus

2017 ◽  
Vol 73 (a2) ◽  
pp. C1296-C1296
Author(s):  
Bryan Trevor Sewell ◽  
Achilleas Frangakis ◽  
Andani Mulelu ◽  
Julian Reitz
Keyword(s):  
Bacillus Pumilus ◽  
Cyanide Dihydratase

Enhancement in catalytic activity of CotA-laccase from Bacillus pumilus W3 via site-directed mutagenesis

2020 ◽  
Vol 129 (4) ◽  
pp. 405-411 ◽  
Author(s):  
Kai-Zhong Xu ◽  
Hao-Ran Wang ◽  
Ya-Jing Wang ◽  
Jing Xia ◽  
Hui Ma ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Bacillus Pumilus ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Cota Laccase

Residue Y70 of the Nitrilase Cyanide Dihydratase from Bacillus pumilus Is Critical for Formation and Activity of the Spiral Oligomer

2016 ◽  
Vol 26 (12) ◽  
pp. 2179-2183
Author(s):  
Jason M. Park ◽  
Christian M. Ponder ◽  
B. Trevor Sewell ◽  
Michael J. Benedik
Keyword(s):  
Bacillus Pumilus ◽  
Cyanide Dihydratase

High resolution electron microscopy of lanthanum phosphate crystals

1978 ◽  
Vol 36 (1) ◽  
pp. 274-275
Author(s):  
J. C. Wheatley ◽  
J. M. Cowley
Keyword(s):  
Electron Microscopy ◽  
Catalytic Activity ◽  
High Resolution ◽  
Petroleum Industry ◽  
High Resolution Electron Microscopy ◽  
Lanthanum Phosphate ◽  
Good Catalyst ◽  
Resolution Electron ◽  
Good Catalytic Activity ◽  
Physical And Chemical

Rare-earth phosphates are of particular interest because of their catalytic properties associated with the hydrolysis of many aromatic chlorides in the petroleum industry. Lanthanum phosphates (LaPO4) which have been doped with small amounts of copper have shown increased catalytic activity (1). However the physical and chemical characteristics of the samples leading to good catalytic activity are not known.Many catalysts are amorphous and thus do not easily lend themselves to methods of investigation which would include electron microscopy. However, the LaPO4, crystals are quite suitable samples for high resolution techniques.The samples used were obtained from William L. Kehl of Gulf Research and Development Company. The electron microscopy was carried out on a JEOL JEM-100B which had been modified for high resolution microscopy (2). Standard high resolution techniques were employed. Three different sample types were observed: 669A-1-5-7 (poor catalyst), H-L-2 (good catalyst) and 27-011 (good catalyst).

The design and catalytic performance of molybdenum active sites on an MCM-41 framework for the aerobic oxidation of 5-hydroxymethylfurfural to 2,5-diformylfuran

2019 ◽  
Vol 9 (3) ◽  
pp. 811-821 ◽  
Author(s):  
Zhao-Meng Wang ◽  
Li-Juan Liu ◽  
Bo Xiang ◽  
Yue Wang ◽  
Ya-Jing Lyu ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Active Sites ◽  
Aerobic Oxidation ◽  
Catalytic Performance ◽  
Mcm 41

The catalytic activity decreases as –(SiO)3Mo(OH)(O) > –(SiO)2Mo(O)2 > –(O)4–MoO.

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