| dc.creator |
García, José Luis |
|
| dc.creator |
Hormigo, Daniel |
|
| dc.creator |
Stuart, Maribel |
|
| dc.creator |
Arroyo, Miguel |
|
| dc.creator |
Torres, Pedro |
|
| dc.creator |
Torres-Bacete, Jesús |
|
| dc.creator |
Castillón, María Pilar |
|
| dc.creator |
Acebal, Carmen |
|
| dc.creator |
Mata, Isabel de la |
|
| dc.date |
2008-02-06T12:15:35Z |
|
| dc.date |
2008-02-06T12:15:35Z |
|
| dc.date |
2007-06-22 |
|
| dc.date.accessioned |
2017-01-31T00:59:58Z |
|
| dc.date.available |
2017-01-31T00:59:58Z |
|
| dc.identifier |
Appl Environ Microbiol. 2007 August; 73(16): 5378–5381 |
|
| dc.identifier |
PMCID: 1950969 |
|
| dc.identifier |
http://hdl.handle.net/10261/2874 |
|
| dc.identifier |
10.1128/AEM.00452-07 |
|
| dc.identifier.uri |
http://dspace.mediu.edu.my:8181/xmlui/handle/10261/2874 |
|
| dc.description |
We express our gratitude to J. A. Salas from the University of Oviedo for providing the pEM4 expression vector. |
|
| dc.description |
Aculeacin A acylase from Actinoplanes utahensis produced by Streptomyces lividans revealed acylase activities that are able to hydrolyze penicillin V and several natural aliphatic penicillins. Penicillin K was the best substrate, showing a catalytic efficiency of 34.79 mM−1 s−1. Furthermore, aculeacin A acylase was highly thermostable, with a midpoint transition temperature of 81.5°C. |
|
| dc.description |
This work was supported by grant BIO 2003-04832 from the Spanish Ministry of Education and Science. |
|
| dc.description |
Peer reviewed |
|
| dc.format |
429459 bytes |
|
| dc.format |
application/pdf |
|
| dc.language |
eng |
|
| dc.publisher |
American Society for Microbiology |
|
| dc.rights |
openAccess |
|
| dc.title |
Newly Discovered Penicillin Acylase Activity of Aculeacin A Acylase from Actinoplanes utahensis |
|
| dc.type |
Artículo |
|