PMID:12773152: Difference between revisions

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<span style = 'font-size: large'> '''Hunter, WN, Bond, CS, Gabrielsen, M and Kemp, LE'''  (2003) Structure and reactivity in the non-mevalonate pathway of isoprenoid biosynthesis.''Biochem. Soc. Trans.'' '''31''':537-42</span>
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|{{TableHeadingColor}} |'''Abstract''' || The function, structure and mechanism of two Escherichia coli enzymes involved in the non-mevalonate route of isoprenoid biosynthesis, 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase and 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, are reviewed. Comparisons of each with enzymes from microbial pathogens highlight important conservation of sequence suggestive of similarities in secondary structure, subunit folds, quaternary structure and active sites. Since both enzymes are validated drug targets, the models provide templates for structure-based design of anti-microbial agents targeting a number of serious human diseases.
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'''No author listed'''  (2003) Structure and reactivity in the non-mevalonate pathway of isoprenoid biosynthesis. ''Biochem. Soc. Trans.'' '''31''':537-42
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!align=left  |Abstract
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The function, structure and mechanism of two Escherichia coli enzymes involved in the non-mevalonate route of isoprenoid biosynthesis, 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase and 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, are reviewed. Comparisons of each with enzymes from microbial pathogens highlight important conservation of sequence suggestive of similarities in secondary structure, subunit folds, quaternary structure and active sites. Since both enzymes are validated drug targets, the models provide templates for structure-based design of anti-microbial agents targeting a number of serious human diseases.
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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=12773152 PubMed]
Online version:[http://dx.doi.org/10.1042/ 10.1042/]
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12773152 PubMed]
!align=left  |Keywords
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Amino Acid Sequence; Binding Sites; Escherichia coli/enzymology; Insect Proteins/chemistry; Insect Proteins/metabolism; Mevalonic Acid/metabolism; Models, Molecular; Protein Conformation; Protein Prenylation/physiology; Sequence Alignment
 
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==Significance {{HelpIcon|Help:Literature}} ==
==Significance {{HelpIcon|Help:Literature}} ==
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{{LitSignificance}}

Revision as of 18:21, 1 September 2013

Citation

No author listed (2003) Structure and reactivity in the non-mevalonate pathway of isoprenoid biosynthesis. Biochem. Soc. Trans. 31:537-42

Abstract

The function, structure and mechanism of two Escherichia coli enzymes involved in the non-mevalonate route of isoprenoid biosynthesis, 2C-methyl-D-erythritol 4-phosphate cytidylyltransferase and 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, are reviewed. Comparisons of each with enzymes from microbial pathogens highlight important conservation of sequence suggestive of similarities in secondary structure, subunit folds, quaternary structure and active sites. Since both enzymes are validated drug targets, the models provide templates for structure-based design of anti-microbial agents targeting a number of serious human diseases.

Links

PubMed Online version:10.1042/

Keywords

Amino Acid Sequence; Binding Sites; Escherichia coli/enzymology; Insect Proteins/chemistry; Insect Proteins/metabolism; Mevalonic Acid/metabolism; Models, Molecular; Protein Conformation; Protein Prenylation/physiology; Sequence Alignment

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