6.3.2.45: UDP-N-acetylmuramate-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase

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For detailed information about UDP-N-acetylmuramate-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase, go to the full flat file.

Reaction

Synonyms

Mpl, murein peptide ligase, UDP-MurNAc:L-Ala-gamma-D-Glu-meso-A2pm ligase, UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase, UDP-N-alpha-D-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate (ADP-forming), yjfG

ECTree

     6 Ligases

         6.3 Forming carbon-nitrogen bonds

             6.3.2 Acid—amino-acid ligases (peptide synthases)

                6.3.2.45 UDP-N-acetylmuramate-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase

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Results	in table
8533	AA Sequence
2	Cloned(Commentary)
2	General Information
8	kcat/KM [mM/s]
8	KM Value [mM]
1	Metals/Ions
3	Molecular Weight [Da]
1	Natural Substrates/ Products (Substrates)
3	Organism
2	Pathway
2	pH Optimum
1	pH Range
1	Purification (Commentary)
1	Reaction
3	Reference
1	Specific Activity [micromol/min/mg]
11	Substrates and Products (Substrate)
3	Subunits
6	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
8	Turnover Number [1/s]

Natural Substrates Products

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Natural Substrates Products on EC 6.3.2.45 - UDP-N-acetylmuramate-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

ATP + UDP-N-alpha-D-acetylmuramate + L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate

ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate

Escherichia coli

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the recycling enzyme allows reincorporation into peptidoglycan (murein) of the tripeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate released during the maturation and constant remodeling of this bacterial cell wall polymer that occur during cell growth and division. The enzyme adds this peptide to UDP-N-acetylmuramate, thereby providing an economical additional source of UDP-MurNAc-tripeptide available for de novo peptidoglycan biosynthesis

674330

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