dc.contributor.author |
Thuku, RN
|
|
dc.contributor.author |
Brady, D
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|
dc.contributor.author |
Benedik, MJ
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dc.contributor.author |
Sewell, BT
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dc.date.accessioned |
2009-04-14T12:49:37Z |
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dc.date.available |
2009-04-14T12:49:37Z |
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dc.date.issued |
2009-03 |
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dc.identifier.citation |
Thuku, RN, Brady, D, Benedik, MJ and Sewell, BT. 2009. Microbial nitrilases: versatile, spiral forming, industrial enzymes. Journal of Applied Microbiology, Vol. 106(3), pp 1-48 |
en |
dc.identifier.issn |
1364-5072 |
|
dc.identifier.uri |
http://hdl.handle.net/10204/3310
|
|
dc.description |
Copyright: 2008 Blackwell Publishing |
en |
dc.description.abstract |
The nitrilases are enzymes that convert nitriles to the corresponding acid and ammonia. They are members of a superfamily, which includes amidases and occur in both prokaryotes and eukaryotes. The superfamily is characterized by having a homodimeric building block with a abba–abba sandwich fold and an active site containing four positionally conserved residues: cys, glu, glu and lys. Their high chemical specificity and frequent enantioselectivity makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation. The superfamily enzymes have been visualized as dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers and variable length helices, but all nitrilase oligomers have the same basic dimer interface. Moreover, in the case of the octamers, tetradecamers, octadecamers and the helices, common principles of subunit association apply. While the range of industrially interesting reactions catalysed by this enzyme class continues to increase, research efforts are still hampered by the lack of a high resolution microbial nitrilase structure which can provide insights into their specificity, enantioselectivity and the mechanism of catalysis. This review provides an overview of the current progress in elucidation of structure and function in this enzyme class and emphasizes insights that may lead to further biotechnological application |
en |
dc.language.iso |
en |
en |
dc.publisher |
Blackwell Publishing |
en |
dc.subject |
Nitrilase |
en |
dc.subject |
Helical enzymes |
en |
dc.subject |
Oligomer |
en |
dc.subject |
Spiral enzymes |
en |
dc.subject |
Nitrilase superfamily |
en |
dc.subject |
Microbial nitrilases |
en |
dc.subject |
Industrial enzymes |
en |
dc.subject |
Microbiology |
en |
dc.title |
Microbial nitrilases: versatile, spiral forming, industrial enzymes |
en |
dc.type |
Article |
en |
dc.identifier.apacitation |
Thuku, R., Brady, D., Benedik, M., & Sewell, B. (2009). Microbial nitrilases: versatile, spiral forming, industrial enzymes. http://hdl.handle.net/10204/3310 |
en_ZA |
dc.identifier.chicagocitation |
Thuku, RN, D Brady, MJ Benedik, and BT Sewell "Microbial nitrilases: versatile, spiral forming, industrial enzymes." (2009) http://hdl.handle.net/10204/3310 |
en_ZA |
dc.identifier.vancouvercitation |
Thuku R, Brady D, Benedik M, Sewell B. Microbial nitrilases: versatile, spiral forming, industrial enzymes. 2009; http://hdl.handle.net/10204/3310. |
en_ZA |
dc.identifier.ris |
TY - Article
AU - Thuku, RN
AU - Brady, D
AU - Benedik, MJ
AU - Sewell, BT
AB - The nitrilases are enzymes that convert nitriles to the corresponding acid and ammonia. They are members of a superfamily, which includes amidases and occur in both prokaryotes and eukaryotes. The superfamily is characterized by having a homodimeric building block with a abba–abba sandwich fold and an active site containing four positionally conserved residues: cys, glu, glu and lys. Their high chemical specificity and frequent enantioselectivity makes them attractive biocatalysts for the production of fine chemicals and pharmaceutical intermediates. Nitrilases are also used in the treatment of toxic industrial effluent and cyanide remediation. The superfamily enzymes have been visualized as dimers, tetramers, hexamers, octamers, tetradecamers, octadecamers and variable length helices, but all nitrilase oligomers have the same basic dimer interface. Moreover, in the case of the octamers, tetradecamers, octadecamers and the helices, common principles of subunit association apply. While the range of industrially interesting reactions catalysed by this enzyme class continues to increase, research efforts are still hampered by the lack of a high resolution microbial nitrilase structure which can provide insights into their specificity, enantioselectivity and the mechanism of catalysis. This review provides an overview of the current progress in elucidation of structure and function in this enzyme class and emphasizes insights that may lead to further biotechnological application
DA - 2009-03
DB - ResearchSpace
DP - CSIR
KW - Nitrilase
KW - Helical enzymes
KW - Oligomer
KW - Spiral enzymes
KW - Nitrilase superfamily
KW - Microbial nitrilases
KW - Industrial enzymes
KW - Microbiology
LK - https://researchspace.csir.co.za
PY - 2009
SM - 1364-5072
T1 - Microbial nitrilases: versatile, spiral forming, industrial enzymes
TI - Microbial nitrilases: versatile, spiral forming, industrial enzymes
UR - http://hdl.handle.net/10204/3310
ER -
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en_ZA |