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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
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MetaCyc Enzyme: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligase

Gene: murE Accession Numbers: G-12446 (MetaCyc), TM_0237

Species: Thermotoga maritima

Summary:
The peptidoglycan of Thermotoga maritima contains no meso-diaminopimelate and approximately equal amounts of L- and D-lysine The murE gene of Thermotoga maritima was cloned in Escherichia coli, and the corresponding protein was purified as the C-terminal His6-tagged form [Boniface06]. The purified recombinant enzyme added D-lysine and meso-diaminopimelate to UDP-N-acetylmuramoyl-L-alanyl--D-glutamate with 25 and 10% efficiencies, respectively, relative to L-lysine.

The D-lysine residue is added in a different manner than the L-lysine residue, and is attached to the D-glutamate residue by its epsilon-amino function. The product was not a substrate for MurF, but could be directly attached to a lipid anchor by the phospho-N-acetylmuramoyl-pentapeptide-transferase MraY (EC 2.7.8.13) [Boniface06].

Molecular Weight of Polypeptide: 54.74 kD (from nucleotide sequence)

Unification Links: Entrez-gene:897137 , Pride:Q9WY79 , Protein Model Portal:Q9WY79 , String:243274.TM0237 , UniProt:Q9WY79

Relationship Links: InterPro:IN-FAMILY:IPR000713 , InterPro:IN-FAMILY:IPR004101 , InterPro:IN-FAMILY:IPR005761 , InterPro:IN-FAMILY:IPR013221 , InterPro:IN-FAMILY:IPR018109 , PDB:Structure:4BUB , Pfam:IN-FAMILY:PF01225 , Pfam:IN-FAMILY:PF02875 , Pfam:IN-FAMILY:PF08245

Gene-Reaction Schematic: ?

Credits:
Created 13-Jan-2011 by Caspi R , SRI International


Enzymatic reaction of: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligase)

EC Number: 6.3.2.7

UDP-N-acetylmuramoyl-L-alanyl--D-glutamate + L-lysine + ATP <=> UDP-N-acetylmuramoyl-L-alanyl-γ-D-glutamyl-L-lysine + ADP + phosphate + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Kinetic Parameters:

Substrate
Km (μM)
Citations
L-lysine
2800.0
[Boniface06]
UDP-N-acetylmuramoyl-L-alanyl--D-glutamate
450.0
[Boniface06]

T(opt): 68 °C [Boniface06]

pH(opt): 9.4 [Boniface06]


Enzymatic reaction of: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--D-lysine ligase (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--LD-lysine ligase)

EC Number: 6.3.2.37

UDP-N-acetylmuramoyl-L-alanyl--D-glutamate + D-lysine + ATP <=> UDP-N-acetylmuramoyl-L-alanyl-γ-D-glutamyl-D-lysine + ADP + phosphate + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.


References

Boniface06: Boniface A, Bouhss A, Mengin-Lecreulx D, Blanot D (2006). "The MurE synthetase from Thermotoga maritima is endowed with an unusual D-lysine adding activity." J Biol Chem 281(23);15680-6. PMID: 16595662


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, biocyc14.