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Literature summary for 6.3.2.9 extracted from

  • Bratkovic, T.; Lunder, M.; Urleb, U.; Strukelj, B.
    Peptide inhibitors of MurD and MurE, essential enzymes of bacterial cell wall biosynthesis (2008), J. Basic Microbiol., 48, 202-206.
    View publication on PubMed

Application

Application Comment Organism
drug development MurD is a target for small molecule chemotherapeutics Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
CPAHWPHPC i.e. peptide MD-C7C_1, inhibits MurD Escherichia coli
CSAWSNKFC i.e. peptide MD-C7C_2, inhibits MurD Escherichia coli
HSSWYIQHFPPL i.e. peptide MD-12, inhibits MurD Escherichia coli
additional information design of peptidomimetic lead compounds with the ultimate objective of small molecule chemotherapeutic development, affinity selection by immobilized MurD with addition of ATP in an attempt to achieve conformationally homogenous population of target enzymes, overview. No inhibition by peptide MD-C7C_3, i.e. CQSSPHMSC Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Escherichia coli 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate Escherichia coli MurD is essential for cytoplasmic bacterial cell wall biosynthesis ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
gene murD
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate
-
Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
?
ATP + UDP-N-acetylmuramyl-L-alanine + D-glutamate MurD is essential for cytoplasmic bacterial cell wall biosynthesis Escherichia coli ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-glutamate
-
?

Subunits

Subunits Comment Organism
More all Mur ligases are topologically similar to each other, extremely flexible, and built of three domains connected by two hinges. Each domain binds one of the three substrates, i.e. ATP, growing nucleotide, or the appropriate amino acid Escherichia coli

Synonyms

Synonyms Comment Organism
MurD
-
Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.14
-
pH 8.0, 37°C Escherichia coli HSSWYIQHFPPL
0.62
-
pH 8.0, 37°C Escherichia coli CSAWSNKFC
1.5
-
pH 8.0, 37°C Escherichia coli CPAHWPHPC