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Literature summary extracted from

  • Brandish, P.E.; Burnham, M.K.; Lonsdale, J.T.; Southgate, R.; Inukai, M.; Bugg, T.D.H.
    Slow binding inhibition of phospho-N-acetylmuramyl-pentapeptide-translocase (Escherichia coli) by mureidomycin A (1996), J. Biol. Chem., 271, 7609-7614.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.8.13 phosphatidylglycerol activity is stimulated 5-10fold by inclusion of 0.1 mg/ml in both radiochemical and fluorescence enhancement assays Escherichia coli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.8.13 overexpressed in recombinant Escherichia coli JM109 Escherichia coli

General Stability

EC Number General Stability Organism
2.7.8.13 no loss of activity observed upon gel filtration, desalted enzyme is completely inactive Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.8.13 mureidomycin A
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.8.13 0.013
-
dodecaprenylphosphate pH 7.5, 30°C Escherichia coli
2.7.8.13 0.019
-
dansyl-UDP-NAc-muramoyl-pentapeptide pH 7.5, 30°C Escherichia coli
2.7.8.13 0.019
-
heptaprenylphosphate pH 7.5, 30°C Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.8.13 Mg2+ can be replaced only by Mn2+ Escherichia coli
2.7.8.13 additional information no activity is observed using Ni2+, Ca2+ and Zn2+ Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.8.13 35000 45000 SDS-PAGE Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.8.13 UDP-MurNAc-pentapeptide + undecaprenyl-phosphate Escherichia coli natural acceptor UMP + MurNAc-pentapeptide diphosphoryl undecaprenol
-
r
2.7.8.13 UDP-NAc-muramoyl-pentapeptide + acceptor Escherichia coli biosynthesis of peptidoglycan, first lipid intermediate UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
r
2.7.8.13 UDP-NAc-muramoyl-pentapeptide + acceptor Escherichia coli JM105 biosynthesis of peptidoglycan, first lipid intermediate UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.13 Escherichia coli
-
wild-type JM105
-
2.7.8.13 Escherichia coli JM105
-
wild-type JM105
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.8.13 additional information
-
specific activity is increased 2fold by induction with isopropyl-beta-D-thiogalactopyranoside in the late logarithmic phase Escherichia coli
2.7.8.13 additional information
-
0.42 units, using fluorescence enhancement assay, recombinant strain JM109 (pTrc99A), 11.9 units, recombinant strain JM109 (pBROC525), activity is expressed as increase in units of fluorescence emission per min at 30°C Escherichia coli
2.7.8.13 0.000276
-
specific activity of particulate enzyme from recombinant strain JM109 (pBROC525), in absence of exogenous lipid acceptor Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.8.13 dansyl-UDP-NAc-muramoyl-pentapeptide + undecaprenyl phosphate
-
Escherichia coli UMP + dansyl-UDP-NAc-muramoyl-pentapeptide-diphosphoundecaprenol
-
?
2.7.8.13 UDP-MurNAc(oyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelyl-(N-dansyl)-D-Ala-D-Ala) + dodecaprenyl phosphate dPP Escherichia coli UMP + MurNAc(oyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelyl-(N-dansyl)-D-Ala-D-Ala)-diphosphododecaprenol
-
r
2.7.8.13 UDP-MurNAc(oyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelyl-(N-dansyl)-D-Ala-D-Ala) + dodecaprenyl phosphate dPP Escherichia coli JM105 UMP + MurNAc(oyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelyl-(N-dansyl)-D-Ala-D-Ala)-diphosphododecaprenol
-
r
2.7.8.13 UDP-MurNAc-pentapeptide + undecaprenoid-1-ol-phosphate
-
Escherichia coli lipid-P-P-MurNAc-pentapeptide + UMP
-
r
2.7.8.13 UDP-MurNAc-pentapeptide + undecaprenoid-1-ol-phosphate
-
Escherichia coli JM105 lipid-P-P-MurNAc-pentapeptide + UMP
-
r
2.7.8.13 UDP-MurNAc-pentapeptide + undecaprenyl-phosphate natural acceptor Escherichia coli UMP + MurNAc-pentapeptide diphosphoryl undecaprenol
-
r
2.7.8.13 UDP-NAc-muramoyl-pentapeptide + acceptor
-
Escherichia coli UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
r
2.7.8.13 UDP-NAc-muramoyl-pentapeptide + acceptor biosynthesis of peptidoglycan, first lipid intermediate Escherichia coli UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
r
2.7.8.13 UDP-NAc-muramoyl-pentapeptide + acceptor
-
Escherichia coli JM105 UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
r
2.7.8.13 UDP-NAc-muramoyl-pentapeptide + acceptor biosynthesis of peptidoglycan, first lipid intermediate Escherichia coli JM105 UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
r
2.7.8.13 UDP-NAc-muramoyl-pentapeptide + dodecaprenyl-phosphate dodecaprenyl phosphate is a more efficient substrate than heptaprenyl-phosphate, enzyme is selective for larger substrate which is closer in chain length to the natural substrate, undecaprenyl-phosphate Escherichia coli UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
r
2.7.8.13 UDP-NAc-muramoyl-pentapeptide + dodecaprenyl-phosphate dodecaprenyl phosphate is a more efficient substrate than heptaprenyl-phosphate, enzyme is selective for larger substrate which is closer in chain length to the natural substrate, undecaprenyl-phosphate Escherichia coli JM105 UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
r
2.7.8.13 UDP-NAc-muramoyl-pentapeptide + heptaprenyl-phosphate
-
Escherichia coli UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
r

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.8.13 0.000036
-
mureidomycin A pH 7.5, 30°C Escherichia coli