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Mutation of Gln125 to Asn selectively abolishes the thymidylate kinase activity of herpes simplex virus type 1 thymidine kinase.

Abstract:

The broad substrate specificity of herpes simplex virus type 1 (HSV-1) thymidine kinase (TK) has provided the basis for selective antiherpetic therapy and, more recently, suicide gene therapy for the treatment of cancer. We have now constructed an HSV-1 TK mutant enzyme, in which an asparagine (N) residue is substituted for glutamine (Q) at position 125, and have evaluated the effect of this amino acid change on enzymatic activity. In marked contrast with wild-type HSV-1 TK, which displays bo...

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Publication status:
Published

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Journal:
Molecular pharmacology More from this journal
Volume:
59
Issue:
2
Pages:
285-293
Publication date:
2001-02-01
EISSN:
1521-0111
ISSN:
0026-895X
Language:
English
Keywords:
Pubs id:
pubs:20676
UUID:
uuid:fda6d61d-1baf-4e0b-acf4-40992c5014ee
Local pid:
pubs:20676
Source identifiers:
20676
Deposit date:
2012-12-19

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