PMID:2171503: Difference between revisions
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| | !align=left |Citation | ||
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'''No author listed''' (1990) Role of cysteine residues in ribonuclease H from Escherichia coli. Site-directed mutagenesis and chemical modification. ''Biochem. J.'' '''271''':59-66 | |||
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| | !align=left |Abstract | ||
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The role of the three cysteine residues at positions 13, 63 and 133 in Escherichia coli RNAase H, an enzyme that is sensitive to N-ethylmaleimide [Berkower, Leis & Hurwitz (1973) J. Biol. Chem. 248, 5914-5921], was examined by using both site-directed mutagenesis and chemical modification. Novel aspects that were found are as follows. First, none of the cysteine residues is required for activity. Secondly, chemical modification of either Cys-13 or Cys-133 with thiol-blocking reagents inactivates the enzyme, but that of Cys-63 does not. Thus the sensitivity of E. coli RNAase H to N-ethylmaleimide arises not from blocking of the thiol group but from steric hindrance by the modifying group incorporated at either Cys-13 or Cys-133. | |||
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!align=left |Links | |||
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2171503 PubMed] [http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1150208 PMC1150208] | |||
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!align=left |Keywords | |||
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Amino Acid Sequence; Chemical Phenomena; Chemistry; Chromatography, High Pressure Liquid; Circular Dichroism; Cysteine; Dithionitrobenzoic Acid; Endoribonucleases/antagonists & inhibitors; Endoribonucleases/chemistry; Endoribonucleases/metabolism; Escherichia coli/enzymology; Ethylmaleimide/pharmacology; Iodoacetates/pharmacology; Iodoacetic Acid; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Mapping; Ribonuclease H; Serine Endopeptidases/metabolism; Structure-Activity Relationship | |||
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==Significance {{HelpIcon|Help:Literature}} == | ==Significance {{HelpIcon|Help:Literature}} == | ||
{{LitSignificance}} | {{LitSignificance}} | ||
Revision as of 19:14, 1 September 2013
| Citation |
No author listed (1990) Role of cysteine residues in ribonuclease H from Escherichia coli. Site-directed mutagenesis and chemical modification. Biochem. J. 271:59-66 |
|---|---|
| Abstract |
The role of the three cysteine residues at positions 13, 63 and 133 in Escherichia coli RNAase H, an enzyme that is sensitive to N-ethylmaleimide [Berkower, Leis & Hurwitz (1973) J. Biol. Chem. 248, 5914-5921], was examined by using both site-directed mutagenesis and chemical modification. Novel aspects that were found are as follows. First, none of the cysteine residues is required for activity. Secondly, chemical modification of either Cys-13 or Cys-133 with thiol-blocking reagents inactivates the enzyme, but that of Cys-63 does not. Thus the sensitivity of E. coli RNAase H to N-ethylmaleimide arises not from blocking of the thiol group but from steric hindrance by the modifying group incorporated at either Cys-13 or Cys-133. |
| Links | |
| Keywords |
Amino Acid Sequence; Chemical Phenomena; Chemistry; Chromatography, High Pressure Liquid; Circular Dichroism; Cysteine; Dithionitrobenzoic Acid; Endoribonucleases/antagonists & inhibitors; Endoribonucleases/chemistry; Endoribonucleases/metabolism; Escherichia coli/enzymology; Ethylmaleimide/pharmacology; Iodoacetates/pharmacology; Iodoacetic Acid; Molecular Sequence Data; Mutagenesis, Site-Directed; Peptide Mapping; Ribonuclease H; Serine Endopeptidases/metabolism; Structure-Activity Relationship |
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