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Information on EC 2.7.8.13 - phospho-N-acetylmuramoyl-pentapeptide-transferase
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2.7.8.13 phospho-N-acetylmuramoyl-pentapeptide-transferaseIUBMB Comments
In Gram-negative and some Gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-centre. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).
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Word Map
- 2.7.8.13
- peptidoglycan
- capuramycins
- udp-murnac-pentapeptide
-
muraymycins
-
mureidomycins
- medicine
-
pacidamycins
-
caprazamycins
- drug development
- molecular biology
- analysis
- synthesis
The enzyme appears in viruses and cellular organisms
Synonyms
translocase i, translocase 1, phospho-murnac-pentapeptide translocase, mray translocase, phospho-n-acetylmuramyl-pentapeptide translocase, mray transferase, mray protein, phospho-n-acetylmuramoyl-pentapeptide translocase, phospho-n-acetyl-muramyl-pentapeptide translocase, phospho-n-acetylmuramoyl-pentapeptide-transferase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MraY
MraY protein
MraY transferase
MraY translocase
phospho-MurNAc-pentapeptide transferase
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phospho-MurNAc-pentapeptide translocase
phospho-N-acetylmuramoyl pentapeptide translocase
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phospho-N-acetylmuramoyl-pentapeptide translocase
phospho-N-acetylmuramoylpentapeptidetransferase
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phospho-N-acetylmuramyl-pentapeptide translocase
phospho-NAc-muramoyl-pentapeptide translocase (UMP)
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phosphoacetylmuramoylpentapeptide translocase
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phosphoacetylmuramoylpentapeptidetransferase
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polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase
translocase I
translocase-I
UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla:undecaprenylphosphate transferase
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UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala:C55-isoprenoid alcohol transferase
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MraY transferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
in gram-negative and some gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-centre. The undecaprenol involved is ditrans, octacis-undecaprenol
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UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
a one-step, single displacement mechanism. The oxyanion of the polyprenyl-phosphate attacks the b-phosphate of the nucleotide substrate, leading to the formation of product lipid I and liberation of UMP. The involvement of an invariant aspartyl residue in the deprotonation of the lipid substrate is possible. Formation of a covalent reaction intermediate
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate = UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
a one-step, single displacement mechanism. The oxyanion of the polyprenyl-phosphate attacks the b-phosphate of the nucleotide substrate, leading to the formation of product lipid I and liberation of UMP. The involvement of an invariant aspartyl residue in the deprotonation of the lipid substrate is possible. Formation of a covalent reaction intermediate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
substituted phospho group transfer
substituted phospho group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
UDP-MurAc(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala):undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide-transferase
In Gram-negative and some Gram-positive organisms the L-lysine is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm), which is combined with adjacent residues through its L-centre. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).
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CAS REGISTRY NUMBER
COMMENTARY
9068-50-2
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dansyl-UDP-NAc-muramoyl-pentapeptide + undecaprenyl phosphate
UMP + dansyl-UDP-NAc-muramoyl-pentapeptide-diphosphoundecaprenol
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-
-
-
?
N-dansyl-UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
N-fluorescamine-UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
N-o-phthalaldehyde-UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP-MurNAc(oyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelyl-(N-dansyl)-D-Ala-D-Ala) + dodecaprenyl phosphate
UMP + MurNAc(oyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelyl-(N-dansyl)-D-Ala-D-Ala)-diphosphododecaprenol
UDP-MurNAc-(oyl-L-Ala) + undecaprenyl phosphate
UMP + MurNAc(oyl-L-Ala)-diphosphoundecaprenol
UDP-MurNAc-(oyl-L-Ala-gamma-D-Glu) + undecaprenyl phosphate
UMP + MurNAc(oyl-L-Ala-gamma-D-Glu)-diphosphoundecaprenol
36% activity compared to UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)
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r
UDP-MurNAc-(oyl-L-Ala-gamma-D-Glu-meso-diaminopimelate) + undecaprenyl phosphate
UMP + MurNAc(oyl-L-Ala-gamma-D-Glu-meso-diaminopimelate)-diphosphoundecaprenol
51% activity compared to UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)
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r
UDP-MurNAc-Ala-D-Glu-Lys + undecaprenyl phosphate
UMP + MurNAc-Ala-D-Glu-Lys-diphosphoundecaprenol
UDP-MurNAc-Ala-D-Glu-Lys-D-Ala + undecaprenyl phosphate
UMP + MurNAc-Ala-D-Glu-Lys-D-Ala-diphosphoundecaprenol
UDP-MurNAc-Ala-D-Glu-Lys-D-Ala-Gly + undecaprenyl phosphate
UMP + MurNAc-Ala-D-Glu-Lys-D-Ala-Gly-diphosphoundecaprenol
-
-
-
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?
UDP-MurNAc-Ala-D-Glu-Lys-Gly-D-Ala + undecaprenyl phosphate
UMP + MurNAc-Ala-D-Glu-Lys-Gly-D-Ala-diphosphoundecaprenol
-
-
-
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?
UDP-MurNAc-Ala-D-Glu-Orn-D-Ala-D-Ala + undecaprenyl phosphate
UMP + MurNAc-Ala-D-Glu-Orn-D-Ala-D-Ala-diphosphoundecaprenol
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-
-
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?
UDP-MurNAc-Ala-Glu-Lys + undecaprenyl phosphate
UMP + MurNAc-Ala-Glu-Lys-diphosphoundecaprenol
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-
-
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?
UDP-MurNAc-Gly-D-Glu-Lys-D-Ala-D-Ala + undecaprenyl phosphate
UMP + MurNAc-Gly-D-Glu-Lys-D-Ala-D-Ala-diphosphoundecaprenol
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-
-
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?
UDP-MurNAc-L-Ala-gamma-D-Glu-m-DAP-[Nepsilon-dansyl]-D-Ala-D-Ala + undecaprenyl phosphate
UMP + MurNAc-L-Ala-gamma-D-Glu-m-DAP-[Nepsilon-dansyl]-D-Ala-D-Ala-diphosphoundecaprenol
UDP-MurNAc-pentapeptide + C55-isoprenyl phosphate
C55-isoprenyl-diphosphate-MurNAc-pentapeptide
UDP-MurNAc-pentapeptide + undecaprenoid-1-ol-phosphate
lipid-P-P-MurNAc-pentapeptide + UMP
UDP-MurNAc-pentapeptide + undecaprenyl phosphate
UMP + MurNAc-pentapeptide-diphosphoundecaprenol
UDP-MurNAc-pentapeptide + undecaprenyl phosphate
UMP + undecaprenol diphosphate N-acetylmuramyl pentapeptide
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30 min, 35°C, pH 7.5
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?
UDP-MurNAc-pentapeptide + undecaprenyl-phosphate
UMP + MurNAc-pentapeptide diphosphoryl undecaprenol
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP-N-acetylmuramoyl-pentapeptide + undecaprenyl phosphate
?
-
a homogeneous fluorescence resonance energy transfer (FRET)-based assay for the translocase activity of MraY in which the donor fluorophore is attached to UNAM-pp and the acceptor is embedded in detergent micelles containing MraY and undecaprenyl phosphate is described
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?
UDP-N-acetylmuramoyl-pentapeptide + undecaprenyl phosphate
UMP + N-acetylmuramoyl-pentapeptide-diphosphoundecaprenol
25°C, pH 7.2
lipid I synthesis, peptidoglycan biosynthesis
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?
UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
UDP-NAc-muramoyl-pentapeptide + dodecaprenyl-phosphate
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
UDP-NAc-muramoyl-pentapeptide + heptaprenyl-phosphate
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
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r
UDP-NAc-muramoyl-pentapeptide + undecaprenyl phosphate
UMP + undecaprenyl-phospho-NAc-muramoyl-pentapeptide
UDPMur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
N-dansyl-UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
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-
-
-
?
N-dansyl-UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
-
-
-
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?
N-fluorescamine-UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
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-
-
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?
N-fluorescamine-UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
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-
-
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?
N-o-phthalaldehyde-UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
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-
-
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?
N-o-phthalaldehyde-UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
-
-
-
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?
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
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r
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
catalyzes the first membrane step of bacterial cell wall peptidyglycan synthesis
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r
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
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r
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
catalyzes the first membrane step in biosynthesis of bacterial cell wall peptidoglycan
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-
?
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
catalyzes the first membrane step of bacterial cell wall peptidyglycan synthesis
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r
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
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catalyzes the first of a sequence of lipid-linked steps that ultimately assemble the peptidoglycan layer of the bacterial cell wall
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?
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
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r
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
catalyzes the first membrane step of bacterial cell wall peptidyglycan synthesis
-
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r
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
?
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
r
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
the forward and reverse exchange reactions require the presence of the second substrate, undecaprenyl phosphate and UMP, respectively. No activity is detected with isopentenyl phosphate, but the enzyme is highly active with neryl phosphate, heptaprenyl phosphate, dodecaprenyl phosphate, and pentadecaprenyl phosphate
-
-
r
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
?
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
r
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
the forward and reverse exchange reactions require the presence of the second substrate, undecaprenyl phosphate and UMP, respectively. No activity is detected with isopentenyl phosphate, but the enzyme is highly active with neryl phosphate, heptaprenyl phosphate, dodecaprenyl phosphate, and pentadecaprenyl phosphate
-
-
r
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
-
?
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
-
?
UDP-MurNAc + undecaprenyl phosphate
UMP + MurNAc-diphosphoundecaprenol
24% activity compared to UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)
-
-
r
UDP-MurNAc + undecaprenyl phosphate
UMP + MurNAc-diphosphoundecaprenol
24% activity compared to UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)
-
-
r
UDP-MurNAc(oyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelyl-(N-dansyl)-D-Ala-D-Ala) + dodecaprenyl phosphate
UMP + MurNAc(oyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelyl-(N-dansyl)-D-Ala-D-Ala)-diphosphododecaprenol
-
dPP
-
r
UDP-MurNAc(oyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelyl-(N-dansyl)-D-Ala-D-Ala) + dodecaprenyl phosphate
UMP + MurNAc(oyl-L-Ala-gamma-D-Glu-meso-2,6-diaminopimelyl-(N-dansyl)-D-Ala-D-Ala)-diphosphododecaprenol
-
dPP
-
r
UDP-MurNAc-(oyl-L-Ala) + undecaprenyl phosphate
UMP + MurNAc(oyl-L-Ala)-diphosphoundecaprenol
9% activity compared to UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)
-
-
r
UDP-MurNAc-(oyl-L-Ala) + undecaprenyl phosphate
UMP + MurNAc(oyl-L-Ala)-diphosphoundecaprenol
9% activity compared to UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)
-
-
r
UDP-MurNAc-Ala-D-Glu-Lys + undecaprenyl phosphate
UMP + MurNAc-Ala-D-Glu-Lys-diphosphoundecaprenol
-
-
-
-
?
UDP-MurNAc-Ala-D-Glu-Lys + undecaprenyl phosphate
UMP + MurNAc-Ala-D-Glu-Lys-diphosphoundecaprenol
-
-
-
-
?
UDP-MurNAc-Ala-D-Glu-Lys-D-Ala + undecaprenyl phosphate
UMP + MurNAc-Ala-D-Glu-Lys-D-Ala-diphosphoundecaprenol
-
-
-
-
?
UDP-MurNAc-Ala-D-Glu-Lys-D-Ala + undecaprenyl phosphate
UMP + MurNAc-Ala-D-Glu-Lys-D-Ala-diphosphoundecaprenol
-
-
-
-
?
UDP-MurNAc-L-Ala-gamma-D-Glu-m-DAP-[Nepsilon-dansyl]-D-Ala-D-Ala + undecaprenyl phosphate
UMP + MurNAc-L-Ala-gamma-D-Glu-m-DAP-[Nepsilon-dansyl]-D-Ala-D-Ala-diphosphoundecaprenol
-
inhibitory assay
-
-
?
UDP-MurNAc-L-Ala-gamma-D-Glu-m-DAP-[Nepsilon-dansyl]-D-Ala-D-Ala + undecaprenyl phosphate
UMP + MurNAc-L-Ala-gamma-D-Glu-m-DAP-[Nepsilon-dansyl]-D-Ala-D-Ala-diphosphoundecaprenol
-
inhibitory assay
-
-
?
UDP-MurNAc-pentapeptide + C55-isoprenyl phosphate
C55-isoprenyl-diphosphate-MurNAc-pentapeptide
-
-
-
r
UDP-MurNAc-pentapeptide + C55-isoprenyl phosphate
C55-isoprenyl-diphosphate-MurNAc-pentapeptide
-
-
-
r
UDP-MurNAc-pentapeptide + undecaprenoid-1-ol-phosphate
lipid-P-P-MurNAc-pentapeptide + UMP
-
-
-
-
r
UDP-MurNAc-pentapeptide + undecaprenoid-1-ol-phosphate
lipid-P-P-MurNAc-pentapeptide + UMP
-
-
-
-
r
UDP-MurNAc-pentapeptide + undecaprenoid-1-ol-phosphate
lipid-P-P-MurNAc-pentapeptide + UMP
-
-
-
-
r
UDP-MurNAc-pentapeptide + undecaprenoid-1-ol-phosphate
lipid-P-P-MurNAc-pentapeptide + UMP
-
UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala + lipid phosphate, specificity profile towards peptide subunit
-
-
r
UDP-MurNAc-pentapeptide + undecaprenoid-1-ol-phosphate
lipid-P-P-MurNAc-pentapeptide + UMP
-
-
-
-
r
UDP-MurNAc-pentapeptide + undecaprenoid-1-ol-phosphate
lipid-P-P-MurNAc-pentapeptide + UMP
-
UDP-MurNAc-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala + lipid phosphate, specificity profile towards peptide subunit
-
-
r
UDP-MurNAc-pentapeptide + undecaprenyl phosphate
UMP + MurNAc-pentapeptide-diphosphoundecaprenol
Lipid I precursor synthesis, murein biosynthesis
-
-
?
UDP-MurNAc-pentapeptide + undecaprenyl phosphate
UMP + MurNAc-pentapeptide-diphosphoundecaprenol
efficient complementation of enzymatic activity in bacterial strain lacking endogenous MraY
-
-
?
UDP-MurNAc-pentapeptide + undecaprenyl phosphate
UMP + MurNAc-pentapeptide-diphosphoundecaprenol
-
Lipid I precursor synthesis, murein biosynthesis
-
-
?
UDP-MurNAc-pentapeptide + undecaprenyl-phosphate
UMP + MurNAc-pentapeptide diphosphoryl undecaprenol
-
-
-
-
r
UDP-MurNAc-pentapeptide + undecaprenyl-phosphate
UMP + MurNAc-pentapeptide diphosphoryl undecaprenol
-
natural acceptor
-
-
r
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
-
-
-
?
UDP-N-acetylmuramoyl-pentapeptide + [2H]UMP
UMP + [2H]UDP-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-N-acetylmuramoyl-pentapeptide + [2H]UMP
UMP + [2H]UDP-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-N-acetylmuramoyl-pentapeptide + [2H]UMP
UMP + [2H]UDP-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-N-acetylmuramoyl-pentapeptide + [2H]UMP
UMP + [2H]UDP-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-N-acetylmuramoyl-pentapeptide + [2H]UMP
UMP + [2H]UDP-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-N-acetylmuramoyl-pentapeptide + [2H]UMP
UMP + [2H]UDP-NAc-muramoyl-pentapeptide
Priestia megaterium KM / ATCC 13632
-
-
-
r
UDP-N-acetylmuramoyl-pentapeptide + [2H]UMP
UMP + [2H]UDP-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-N-acetylmuramoyl-pentapeptide + [2H]UMP
UMP + [2H]UDP-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-N-acetylmuramoyl-pentapeptide + [2H]UMP
UMP + [2H]UDP-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-N-acetylmuramoyl-pentapeptide + [2H]UMP
UMP + [2H]UDP-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
-
-
-
-
?
UDP-NAc-muramoyl-L-Ala-gamma-D-Glu-meso-diaminopimelic acid-D-Ala-D-Ala + undecaprenyl phosphate
UMP + ?
-
-
-
-
?
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
-
?
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
first step in lipid cycle reactions in biosynthesis of bacterial cell wall peptidoglycans
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
-
?
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
first step in lipid cycle reactions in biosynthesis of bacterial cell wall peptidoglycans
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
Priestia megaterium KM / ATCC 13632
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
equilibrium constant 0.25
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
first step in lipid cycle reactions in biosynthesis of bacterial cell wall peptidoglycans
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
equilibrium constant 0.25
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
first step in lipid cycle reactions in biosynthesis of bacterial cell wall peptidoglycans
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + dodecaprenyl-phosphate
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
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
-
r
UDP-NAc-muramoyl-pentapeptide + dodecaprenyl-phosphate
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
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
-
r
UDP-NAc-muramoyl-pentapeptide + undecaprenyl phosphate
UMP + undecaprenyl-phospho-NAc-muramoyl-pentapeptide
-
-
-
-
?
UDP-NAc-muramoyl-pentapeptide + undecaprenyl phosphate
UMP + undecaprenyl-phospho-NAc-muramoyl-pentapeptide
-
-
-
-
?
UDPMur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
-
r
UDPMur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
catalyzes the first membrane step of bacterial cell wall peptidyglycan synthesis
-
-
r
additional information
?
-
all five cytoplasmic segments contribute to catalytic site with at least 14 invariant polar and/or charged, non-clustered residues, conserved residue D98 supposedly involved in deprotonation of lipid substrate during catalysis at physiological pH 7.4 (pKa for undecaprenyl phosphate: 6.6 and 9.2)
-
-
?
additional information
?
-
-
all five cytoplasmic segments contribute to catalytic site with at least 14 invariant polar and/or charged, non-clustered residues, conserved residue D98 supposedly involved in deprotonation of lipid substrate during catalysis at physiological pH 7.4 (pKa for undecaprenyl phosphate: 6.6 and 9.2)
-
-
?
additional information
?
-
functional complementation in a MraY-lacking, thermosensitive Escherichia coli mutant strain (2fold increased UDP-N-acetylmuramoyl-pentapeptide level compared to wild-type cells when grown 30 min at 42°C, depletion of lipid I) by overexpression of wild-type or mutants E299Q, D177N, N168A, H45R, K48Q, H291R
-
-
?
additional information
?
-
-
functional complementation in a MraY-lacking, thermosensitive Escherichia coli mutant strain (2fold increased UDP-N-acetylmuramoyl-pentapeptide level compared to wild-type cells when grown 30 min at 42°C, depletion of lipid I) by overexpression of wild-type or mutants E299Q, D177N, N168A, H45R, K48Q, H291R
-
-
?
additional information
?
-
assay method development for high-throughput screening assays and metadata annotation, overview
-
-
?
additional information
?
-
the enzyme does not display any diphosphatase activity on the nucleotide substrate. No activity with UDP-GlcNAc and 1-diphospho-MurNAc-pentapeptide. Enzyme catalytic mechanism and substrate specificity, overview. The essential aspartate residue, that is invariant in the superfamily, is Asp98 in Bacillus subtilis MraY, the residue is involved in the deprotonation of the lipid substrate during the catalytic process. UDPMurNAc, UDP-MurNAc-L-Ala, UDP-MurNAc-L-Ala-D-Glu and UDPMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelate precursors of the peptidoglycan biosynthesis pathway are all substrates of the enzyme, no activity with 1-diphospho-MurNAc-pentapeptide. No activity with isopentenyl phosphate as lipid substrate, the enzyme is highly active when tested with neryl phosphate, heptaprenyl phosphate, dodecaprenyl phosphate, and pentadecaprenyl phosphate
-
-
?
additional information
?
-
-
the enzyme does not display any diphosphatase activity on the nucleotide substrate. No activity with UDP-GlcNAc and 1-diphospho-MurNAc-pentapeptide. Enzyme catalytic mechanism and substrate specificity, overview. The essential aspartate residue, that is invariant in the superfamily, is Asp98 in Bacillus subtilis MraY, the residue is involved in the deprotonation of the lipid substrate during the catalytic process. UDPMurNAc, UDP-MurNAc-L-Ala, UDP-MurNAc-L-Ala-D-Glu and UDPMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelate precursors of the peptidoglycan biosynthesis pathway are all substrates of the enzyme, no activity with 1-diphospho-MurNAc-pentapeptide. No activity with isopentenyl phosphate as lipid substrate, the enzyme is highly active when tested with neryl phosphate, heptaprenyl phosphate, dodecaprenyl phosphate, and pentadecaprenyl phosphate
-
-
?
additional information
?
-
assay method development for high-throughput screening assays and metadata annotation, overview
-
-
?
additional information
?
-
the enzyme does not display any diphosphatase activity on the nucleotide substrate. No activity with UDP-GlcNAc and 1-diphospho-MurNAc-pentapeptide. Enzyme catalytic mechanism and substrate specificity, overview. The essential aspartate residue, that is invariant in the superfamily, is Asp98 in Bacillus subtilis MraY, the residue is involved in the deprotonation of the lipid substrate during the catalytic process. UDPMurNAc, UDP-MurNAc-L-Ala, UDP-MurNAc-L-Ala-D-Glu and UDPMurNAc-L-Ala-gamma-D-Glu-meso-diaminopimelate precursors of the peptidoglycan biosynthesis pathway are all substrates of the enzyme, no activity with 1-diphospho-MurNAc-pentapeptide. No activity with isopentenyl phosphate as lipid substrate, the enzyme is highly active when tested with neryl phosphate, heptaprenyl phosphate, dodecaprenyl phosphate, and pentadecaprenyl phosphate
-
-
?
additional information
?
-
-
UDP-N-acetylmuramyl-L-alanyl-gamma-D-glutamyl-meso-diaminopimelyl-D-alanyl-D-alanine: Parks nucleotide, UDP-MurNAc-pentapeptide
-
-
?
additional information
?
-
-
catalyzes an exchange reaction between UMP and UDP-MurNAc-pentapeptide in the absence of undecaprenyl phosphate
-
-
?
additional information
?
-
-
catalyzes an exchange reaction between UMP and UDP-MurNAc-pentapeptide in the absence of undecaprenyl phosphate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP-MurNAc-pentapeptide + undecaprenyl phosphate
UMP + MurNAc-pentapeptide-diphosphoundecaprenol
UDP-MurNAc-pentapeptide + undecaprenyl-phosphate
UMP + MurNAc-pentapeptide diphosphoryl undecaprenol
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
UDPMur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
catalyzes the first membrane step of bacterial cell wall peptidyglycan synthesis
-
-
r
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
catalyzes the first membrane step of bacterial cell wall peptidyglycan synthesis
-
-
r
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
catalyzes the first membrane step in biosynthesis of bacterial cell wall peptidoglycan
-
-
?
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
catalyzes the first membrane step of bacterial cell wall peptidyglycan synthesis
-
-
r
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
catalyzes the first of a sequence of lipid-linked steps that ultimately assemble the peptidoglycan layer of the bacterial cell wall
-
-
?
UDP-Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-D-gamma-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
catalyzes the first membrane step of bacterial cell wall peptidyglycan synthesis
-
-
r
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
r
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
r
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
-
?
UDP-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala) + undecaprenyl phosphate
UMP + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
-
?
UDP-MurNAc-pentapeptide + undecaprenyl phosphate
UMP + MurNAc-pentapeptide-diphosphoundecaprenol
Lipid I precursor synthesis, murein biosynthesis
-
-
?
UDP-MurNAc-pentapeptide + undecaprenyl phosphate
UMP + MurNAc-pentapeptide-diphosphoundecaprenol
-
Lipid I precursor synthesis, murein biosynthesis
-
-
?
UDP-MurNAc-pentapeptide + undecaprenyl-phosphate
UMP + MurNAc-pentapeptide diphosphoryl undecaprenol
-
-
-
-
r
UDP-MurNAc-pentapeptide + undecaprenyl-phosphate
UMP + MurNAc-pentapeptide diphosphoryl undecaprenol
-
natural acceptor
-
-
r
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
-
-
-
?
UDP-N-acetyl-alpha-D-glucosamine + ditrans,octacis-undecaprenyl phosphate
UMP + N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
-
-
-
?
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
first step in lipid cycle reactions in biosynthesis of bacterial cell wall peptidoglycans
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
first step in lipid cycle reactions in biosynthesis of bacterial cell wall peptidoglycans
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
Priestia megaterium KM / ATCC 13632
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
-
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
first step in lipid cycle reactions in biosynthesis of bacterial cell wall peptidoglycans
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
initial stage in peptidoglycan synthesis, key role in selecting analogs of UDP-MurNAc-Ala-gammaDGlu-Lys-DAla-DAla, membrane associated reaction of cell wall biosynthesis
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
first step in lipid cycle reactions in biosynthesis of bacterial cell wall peptidoglycans
-
r
UDP-NAc-muramoyl-pentapeptide + acceptor
UMP + acceptor-phospho-NAc-muramoyl-pentapeptide
-
biosynthesis of peptidoglycan, first lipid intermediate
-
r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
Mg2+
-
absolute requirement for divalent cations, optimal activity with Mg2+ at concentrations 40-75 mM
Mg2+
optimum concentration for wild-type activity: 30-60 mM, inhibitory above 100 mM, 2% of optimum activity left at 250 mM for wild-type and 30-70% for mutants (except mutant E299Q)
Mn2+
-
enzyme activity in presence of Mn2+ is 1% of the activity detected in presence of Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5'-O-(5-amino-5-deoxy-beta-D-ribofuranosyl)-3'-deoxy-3',3'-difluorouridine
-
low inhibition (29% at 11.4 mM), analogue of a liposidomycin (potent and selective inhibitor) assembled from lactol and gem-difluoromethylenated nucleoside with 1,2-trans-beta-furanoside linkage
CPZEN-45
CPZEN-45 strongly inhibits incorporation of radiolabeled glycerol into growing cultures and shows antibacterial activity against caprazamycin-resistant strains, including a strain overexpressing translocase-I MraY, involved in the biosynthesis of peptidoglycan, the target of the caprazamycins. Very poor inhibition by vancomycin
N-(uracilylpentyl)-beta-D-O-(5-amino-5-deoxyribosyl)-L-serine
-
synthesis of analogue of naturally occurring inhibitors like liposidomycins and caprazamycins in which uridine moiety is replaced by a C5 acyclic alkyl chain, and uracil, aminoribose and amino acid moieties are retained
Triton X-100
-
activity is lost upon addition, can be restored by addition of lipid fractions to the assay
3'-O-(2R)-1-(methylamino-1-oxopropan-2-yl)-tunicamycin V
MurNAc analogue of tunicamycin. The inhibitor does not show toxicity against HepG2 cells up to 100 microM, and is a non-toxic selective MraY inhibitor
3'-O-(2R)-1-(methylamino-1-oxopropan-2-yl)-tunicamycin V
MurNAc analogue of tunicamycin. The inhibitordoes not show toxicity against HepG2 cells up to 100 microM, and is a non-toxic selective MraY inhibitor.The inhibitor retains weak antibacterial activity against Staphylococcus aureus, the MIC value is reduced compared to tunicamycin
mureidomycin A
-
inhibitor isolated from Streptomyces flavidovirens WD31235, also antibacterial activity against Pseudomonas aeruginosa A27853
protein E
lysis protein of bacteriophage PhiX174, (strong) binding to MraY leads to cell lysis, overexpression of MraY wild-type rescues bacteria from protein E-induced lysis
-
protein E
-
lysis protein of bacteriophage PhiX174, binding to MraY leads to cell lysis, overexpression of MraY wild-type rescues bacteria from protein E-induced lysis
-
additional information
-
N-lauroyl sarcosine is the best detergent for translocase activity, among different detergents tested CHAPS is the worst for translocase activity
-
additional information
no inhibition by 1-diphospho-N-acetylmuramoyl-pentapeptide
-
additional information
-
no inhibition by 1-diphospho-N-acetylmuramoyl-pentapeptide
-
additional information
-
MraY natural product inhibitors are not broad in spectrum nor practical for general antibiotic use
-
additional information
-
mutant strain, more resistant to tunicamycin than the wild-type
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Moenomycin
-
activates partially purified enzyme, maximal activation at 1 mg moenomycin/mg protein
Neutral lipid
-
stimulates synthesis of C55-isoprenyl-P-P-MurNAc-pentapeptide from UDPMurNAc-pentapeptide, no effect on exchange reaction of UDP-MurNAc-pentapeptide with UMP
-
phosphatidylglycerol
-
activity is stimulated 5-10fold by inclusion of 0.1 mg/ml in both radiochemical and fluorescence enhancement assays
Phospholipid
-
phospholipide sensitive to phospholipase necessary for enzymatic activity
Polar lipid fraction
-
required by exchange reaction of UDP-MurNAc-pentapeptide with UMP
-
Undecaprenyl-diphosphate-MurNAc-pentapeptide
-
stimulates exchange reaction
additional information
-
N-lauroyl sarcosine is the best detergent for translocase activity, among different detergents tested CHAPS is the worst for translocase activity
-
additional information
-
the physical state of the lipid microenvironment of the enzyme has a significant effect on the catalytic activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acidosis, Lactic
Complete loss of expression of the ANT1 gene causing cardiomyopathy and myopathy.
Cardiomyopathy, Dilated
Adenine nucleotide translocase 1 deficiency results in dilated cardiomyopathy with defects in myocardial mechanics, histopathological alterations, and activation of apoptosis.
Cardiomyopathy, Hypertrophic
Complete loss of expression of the ANT1 gene causing cardiomyopathy and myopathy.
Diabetic Cardiomyopathies
Myocardial overexpression of adenine nucleotide translocase 1 ameliorates diabetic cardiomyopathy in mice.
Enterovirus Infections
Adenine nucleotide translocase 1 expression affects enterovirus infection in human and murine hearts.
Heart Diseases
Adenine Nucleotide Translocase 1 Expression is Coupled to the HSP27-Mediated TLR4 Signaling in Cardiomyocytes.
Insulin Resistance
Adenine nucleotide translocase is acetylated in vivo in human muscle: Modeling predicts a decreased ADP affinity and altered control of oxidative phosphorylation.
Mitochondrial Diseases
Complete loss of expression of the ANT1 gene causing cardiomyopathy and myopathy.
Muscular Diseases
Complete loss of expression of the ANT1 gene causing cardiomyopathy and myopathy.
Myalgia
Effects of proteome changes on the tenderness of yak rumen smooth muscle during postmortem storage based on the label-free mass spectrometry.
Neoplasms
Identification of novel inhibitors of phospho-MurNAc-pentapeptide translocase MraY from library screening: Isoquinoline alkaloid michellamine B and xanthene dye phloxine B.
Neoplasms
Over-expression of adenine nucleotide translocase 1 (ANT1) induces apoptosis and tumor regression in vivo.
Parkinson Disease
ADP/ATP translocase 1 protects against an ?-synuclein-associated neuronal cell damage in Parkinson's disease model.
phospho-n-acetylmuramoyl-pentapeptide-transferase deficiency
Adenine nucleotide translocase 1 deficiency results in dilated cardiomyopathy with defects in myocardial mechanics, histopathological alterations, and activation of apoptosis.
Tuberculosis
Activity of capuramycin analogues against Mycobacterium tuberculosis, Mycobacterium avium and Mycobacterium intracellulare in vitro and in vivo.
Tuberculosis
Discovery of a capuramycin analog that kills nonreplicating Mycobacterium tuberculosis and its synergistic effects with translocase I inhibitors.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.022
UDP-MurNAc-Ala-D-Glu-Dap-D-Ala-D-Ala
-
pH 7.8, 37°C, exchange reaction
0.029
UDP-MurNAc-Ala-D-Glu-Lys-D-Ala-Gly
-
pH 7.8, 37°C, exchange reaction
0.1
UDP-MurNAc-Ala-D-Glu-mDap-D-Ala-D-Ala
-
pH 7.8, 37°C, transfer reaction
0.016
UDP-MurNAc-Ala-D-Glu-Orn-D-Ala-D-Ala
-
pH 7.8, 37°C, exchange reaction
0.02
UDP-MurNAc-Ala-D-Glu-Lys-D-Ala-D-Ala
-
pH 7.8, 37°C, exchange reaction
0.055
UDP-MurNAc-Ala-D-Glu-Lys-D-Ala-D-Ala
-
pH 7.8, 37°C, ransfer reaction
0.063
UDP-MurNAc-Ala-D-Glu-Lys-Gly-D-Ala
-
pH 7.8, 37°C, exchange reaction
0.44
UDP-MurNAc-Ala-D-Glu-Lys-Gly-D-Ala
-
pH 7.8, 37°C, transfer reaction
0.044
UDP-MurNAc-Gly-D-Glu-Lys-D-Ala-D-Ala
-
pH 7.8, 37°C, exchange reaction
0.08
UDP-MurNAc-Gly-D-Glu-Lys-D-Ala-D-Ala
-
pH 7.8, 37°C, exchange reaction
0.5
UDP-MurNAc-Gly-D-Glu-Lys-D-Ala-D-Ala
-
pH 7.8, 37°C, transfer reaction
0.087
UDP-MurNAc-pentapeptide
-
pH 7.8, 37°C, at 0.016 mM C55-isoprenylphosphate
additional information
additional information
the enzyme exhibits Michaelis-Menten kinetics towards the heptaprenyl phosphate and dodecaprenyl phosphate lipid substrates. The Km values for dodecaprenyl phosphate and heptaprenyl phosphate are 0.21 mM and 0.15 mM, respectively. The Km values are similar to that of the physiological lipid substrate, undecaprenyl phosphate with 0.16 mM
-
additional information
additional information
-
the enzyme exhibits Michaelis-Menten kinetics towards the heptaprenyl phosphate and dodecaprenyl phosphate lipid substrates. The Km values for dodecaprenyl phosphate and heptaprenyl phosphate are 0.21 mM and 0.15 mM, respectively. The Km values are similar to that of the physiological lipid substrate, undecaprenyl phosphate with 0.16 mM
-
additional information
UDP-N-acetylmuramoyl-pentapeptide
no increase in KM for mutant D98N at pH 9.4 compared to pH 7.2
additional information
UDP-N-acetylmuramoyl-pentapeptide
-
no increase in KM for mutant D98N at pH 9.4 compared to pH 7.2
additional information
undecaprenyl phosphate
3fold increase in KM for mutant D98N at pH 9.4 (ca. 1.2 mM) compared to pH 7.2
additional information
undecaprenyl phosphate
-
3fold increase in KM for mutant D98N at pH 9.4 (ca. 1.2 mM) compared to pH 7.2
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
the enzyme exhibits Michaelis-Menten kinetics towards the heptaprenyl phosphate and dodecaprenyl phosphate lipid substrates. The catalytic constants kcat are 295/min and 54/min, respectively. The kcat for heptaprenyl phosphate is by 6fold lower than those determined for the longer-chain length lipids undecaprenyl phosphate and dodecaprenyl phosphate with 340/min and 295/min, respectively
-
additional information
additional information
-
the enzyme exhibits Michaelis-Menten kinetics towards the heptaprenyl phosphate and dodecaprenyl phosphate lipid substrates. The catalytic constants kcat are 295/min and 54/min, respectively. The kcat for heptaprenyl phosphate is by 6fold lower than those determined for the longer-chain length lipids undecaprenyl phosphate and dodecaprenyl phosphate with 340/min and 295/min, respectively
-
additional information
UDP-N-acetylmuramoyl-pentapeptide
11fold increase in kcat for mutant D98N at pH 9.4 (ca. 0.0083 1/sec) compared to pH 7.2
additional information
UDP-N-acetylmuramoyl-pentapeptide
-
11fold increase in kcat for mutant D98N at pH 9.4 (ca. 0.0083 1/sec) compared to pH 7.2
additional information
undecaprenyl phosphate
11fold increase in kcat for mutant D98N at pH 9.4 (ca. 0.0083 1/sec) compared to pH 7.2
additional information
undecaprenyl phosphate
-
11fold increase in kcat for mutant D98N at pH 9.4 (ca. 0.0083 1/sec) compared to pH 7.2
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000087
3'-O-(2R)-1-(methylamino-1-oxopropan-2-yl)-tunicamycin V
Staphylococcus aureus
pH 7.6, 23°C
0.00005
caprazamycin B
Bacillus subtilis
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.000276
-
specific activity of particulate enzyme from recombinant strain JM109 (pBROC525), in absence of exogenous lipid acceptor
additional information
additional information
-
specific activity is increased 2fold by induction with isopropyl-beta-D-thiogalactopyranoside in the late logarithmic phase
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
additional information
-
assay for MraY by using UDP-MurNAc-Nepsilon-dansylpentapeptide, a fluorescent derivative of the MraY nucleotide substrate. Two assay versions are developed, one consisting of the high-pressure liquid chromatography separation of the substrate and product and the other, without separation and adapted to the high-throughput format, taking advantage of the different fluorescent properties of the nucleotide and lipid I in the reaction medium
additional information
-
specific activity of the enzyme increases 4fold by late-logarithmic phase
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 9
-
activity is significantly weaker at values below pH7.5 or over pH 9.0, about 40% of activity maximum at pH 6.5, about 80% of activity maximum at pH 9.0
6.8 - 9.4
mutant D98N shows different pH profile (specific activity ratio between pH9.4/pH7.6: 2.5) than wild-type (and all mutants except mutant D98N, specific activity ratio between pH9.4/pH7.6: 0.22-0.83)
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
evolution
the enzyme is a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase, P2HPT, superfamily
evolution
-
the enzyme is a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase, P2HPT, superfamily
-
metabolism
the enzyme is involved in the biosynthesis of peptidoglycan
physiological function
-
translocase I is a key enzyme in peptidoglycan biosynthesis
physiological function
-
translocase I is a key enzyme in peptidoglycan biosynthesis
physiological function
enzyme MraY transferase catalyzes the first membrane step of bacterial cell wall peptidoglycan biosynthesis, namely the transfer of the N-acetylmuramoyl-pentapeptide moiety of the cytoplasmic precursor UDP- N-acetylmuramoyl-pentapeptide to the membrane transporter undecaprenyl phosphate (C55-P), yielding undecaprenyl-N-acetylmuramoyl-pentapeptide, i.e. lipid I. The MraY transferase initiates the membrane steps of peptidoglycan biosynthesis and is an essential enzyme for bacterial viability
physiological function
-
enzyme MraY transferase catalyzes the first membrane step of bacterial cell wall peptidoglycan biosynthesis, namely the transfer of the N-acetylmuramoyl-pentapeptide moiety of the cytoplasmic precursor UDP- N-acetylmuramoyl-pentapeptide to the membrane transporter undecaprenyl phosphate (C55-P), yielding undecaprenyl-N-acetylmuramoyl-pentapeptide, i.e. lipid I. The MraY transferase initiates the membrane steps of peptidoglycan biosynthesis and is an essential enzyme for bacterial viability
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100000 - 200000
-
second peak of exchange activity, low molecular weight form, gel filtration
2000000
-
major peak of activity, high molecular weight form, gel filtration
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in the complex with inhibitor muraymycin D2, multiple hydrogen bonds are present in the active site with strength ranging from van der Waals to covalent limits. Lys70, Asp193, Gly194, Asp196, Gly264, Ala321, Gln305, and His325 are key active-site residues interacting with muraymycin D2. Conventional and unconventional hydrogen bonds in addition with charge-dipole and dipole-dipole interactions contribute significantly to stabilize the muraymycin D2 binding
comparison of the human GPT-tunicamycin complex to the MraY-tunicamycin complex. GPT (EC 2.7.8.15) and MraY have drastically different dimer organization and differ in the the role of Mg2+ in tunicamycin inhibition, in active site shape and solvent accessibility and in the lipid substrate specificity
molecular modeling of complex with inhibitor 3'-O-(2R)-1-(methylamino-1-oxopropan-2-yl)-tunicamycin V, the compound generates a steric clash between the N-methylpropanamide moiety introduced in the place of the GlcNAc moiety of 2 and loop E
molecular modeling of complex with inhibitor 3'-O-(2R)-1-(methylamino-1-oxopropan-2-yl)-tunicamycin V, the compound generates a steric clash between the N-methylpropanamide moiety introduced in the place of the GlcNAc moiety of 2 and loop E
molecular modeling of complex with inhibitor 3'-O-(2R)-1-(methylamino-1-oxopropan-2-yl)-tunicamycin V, the compound generates a steric clash between the N-methylpropanamide moiety introduced in the place of the GlcNAc moiety of 2 and loop E
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D174N
0.39% of wild-type activity, 70% of optimum activity in presence of 250 mM Mg2+, altered catalytic efficiency (kcat), not capable of functional complementation, invariant residue in third cytoplasmic segment
D177N
1.6% of wild-type activity, 70% of optimum activity in presence of 250 mM Mg2+, altered catalytic efficiency (kcat), invariant residue in third cytoplasmic segment
D231N
D98A
site-directed mutagenesis, the mutant shows altered pH dependence compared to the wild-type enzyme
D98N
0.014% of wild-type activity, shifted pH optimum (pH 9.0-9.4) compared to wild-type (pH 7.5), highly decreased turnover (kcat, pH 7.2, elevated turnover at pH 9.4), decreased KM for UDP-N-acetylmuramoyl-pentapeptide (pH 7.2 and pH 9.4), increased KM for undecaprenyl phosphate (2fold at pH 7.2, 6fold at pH 9.4), not capable of functional complementation, invariant residue in second cytoplasmic segment
D99N
0.0076% of wild-type activity, highly decreased catalytic efficiency (kcat), increased KM for undecaprenyl phosphate, not capable of functional complementation, invariant residue in second cytoplasmic segment
E299Q
11% of wild-type activity, catalytic activity similarly affected by the presence of 250 mM Mg2+ as wild-type, slightly altered catalytic efficiency (kcat, 10%), invariant residue in fifth cytoplasmic segment
H289R
0.0012% of wild-type activity, highly decreased catalytic efficiency (kcat), not capable of functional complementation, invariant residue in fifth cytoplasmic segment
H290R
0.14% of wild-type activity, altered catalytic efficiency (kcat), not capable of functional complementation, invariant residue in fifth cytoplasmic segment
H291R
0.50% of wild-type activity, altered catalytic efficiency (kcat), increased KM for UDP-N-acetylmuramoyl-pentapeptide, invariant residue in fifth cytoplasmic segment
H45R
0.54% of wild-type activity, 70% of optimum activity in presence of 250 mM Mg2+, altered catalytic efficiency (kcat), increased KM for UDP-N-acetylmuramoyl-pentapeptide, invariant residue in first cytoplasmic segment
K116Q
0.046% of wild-type activity, highly decreased catalytic efficiency (kcat), not capable of functional complementation, invariant residue in second cytoplasmic segment
K48Q
0.51% of wild-type activity, altered catalytic efficiency (kcat), increased KM for UDP-N-acetylmuramoyl-pentapeptide, invariant residue in first cytoplasmic segment
N168A
1.5% of wild-type activity, altered catalytic efficiency (kcat), invariant residue in third cytoplasmic segment
N171A
0.34% of wild-type activity, altered catalytic efficiency (kcat), not capable of functional complementation, invariant residue in third cytoplasmic segment
D98A
-
site-directed mutagenesis, the mutant shows altered pH dependence compared to the wild-type enzyme
-
D267N
deltaL172
-
single-codon deletion in putative transmembrane domain TMD5, mediates PhiX174-resistancy only in catalytically active form and at high culture densitiy
F288L
-
missense mutation in putative transmembrane domain TMD9, mediates PhiX174-resistancy only in catalytically active form
G168S
-
mediates PhiX174-resistancy only at high culture densitiy, similar to wild-type
P170L
-
mediates PhiX174-resistancy only in catalytically active form and at high culture densitiy, interacts with Epos gene product more strongly than with protein E
V291M
-
mediates PhiX174-resistancy only at high culture densitiy, similar to wild-type
D231N
0.42% of wild-type activity, altered catalytic efficiency (kcat), not capable of functional complementation, invariant residue in fourth cytoplasmic segment
D231N
catalytically inactive, overexpression does not rescue bacteria from protein E-induced lysis
D267N
-
enzymatically inactive, overexpression rescues bacteria from protein E-induced lysis
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
no loss of activity observed upon gel filtration, desalted enzyme is completely inactive
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from membrane extracts in presence of DDM detergent and by Ni-NTA metal affinity chromatography
purification using detergent-free styrene-maleic acid copolymer system
solubilization from membrane preparation through shaking for 30 min at 4°C at pH 7.5 and in presence of 1 mM MgCl2 and 2 mM beta-mercaptoethanol
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplification of the mraY gene, previously called open reading frame Y (ORF-Y,1,080 bp) at 2 min in the chromosome map
-
cloning of the murE-dd1B region, the cell wall biosynthesis and cell division gene cluster, expressed in Escherichia coli BL21(DE3)
-
expression of wild-type enzyme and mutant enzymes D115N, D116N and D267N as C-terminal hexahistidine fusion proteins
-
heterologous production in Escherichia coli membranes into styrene-maleic acid-wrapped nanodiscs
His-tagged enzyme, high expression with pET28b expression vector in Escherichia coli BL21(DE3) or C43(DE3), low expression with expression vector pTrc99A in Escherichia coli DH5alpha
in medium-copy plasmid pBAD30 for complementation studies in Escherichia coli K-12 mutant strain RY3321 lacking endogenous MraY
in pET28b for site-directed mutagenesis and expression with N-terminal hexa-His-tag in Escherichia coli C43(DE3) or functional complementation in BW25113-derived thermosensitive strain (EcoliTsMraY) lacking endogenous MraY
His-tagged enzyme, high expression with pET28b expression vector in Escherichia coli BL21(DE3) or C43(DE3), low expression with expression vector pTrc99A in Escherichia coli DH5alpha
-
His-tagged enzyme, high expression with pET28b expression vector in Escherichia coli BL21(DE3) or C43(DE3), low expression with expression vector pTrc99A in Escherichia coli DH5alpha
-
His-tagged enzyme, high expression with pET28b expression vector in Escherichia coli BL21(DE3) or C43(DE3), low expression with expression vector pTrc99A in Escherichia coli DH5alpha
-
His-tagged enzyme, high expression with pET28b expression vector in Escherichia coli BL21(DE3) or C43(DE3), low expression with expression vector pTrc99A in Escherichia coli DH5alpha
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
medicine
molecular biology
-
synthesis of radiolabelled UDP-MurNAc-pentapeptide as biochemical tools for studying peptidoglycan biosynthesis or the kinetic characterization of MraY
synthesis
analysis
the enzyme is an attractive antibacterial drug target involved in peptidoglycan synthesis
analysis
-
the enzyme is an attractive antibacterial drug target involved in peptidoglycan synthesis
-
drug development
antibacterial chemotherapy against pathogenic bacteria being multiresistant to common antibiotics
drug development
-
biological activity of uridine moiety in naturally occurring non-specific MraY inhibitors (like liposidomycins and caprazamycins), antibacterial chemotherapy against pathogenic bacteria being multiresistant to common antibiotics
drug development
the specificity of the enzyme to eubacteria makes it a promising potential target to be exploited for antibacterial discovery to combat emerging resistance
drug development
-
the specificity of the enzyme to eubacteria makes it a promising potential target to be exploited for antibacterial discovery to combat emerging resistance
-
medicine
-
opportunistic pathogen causing infections in patients with burns or neutropenia and involved in respiratory tract infections of cystic fibrosis patients, pathway of peptidoglycan biosynthesis is both essential and unique to bacteria, making it an attractive target for antibiotic research
medicine
-
target for antimicrobial therapeutic intervention, novel antibiotic chemotypes must be developed to deter the alarming rate of antibiotic resistance growth
synthesis
the enzyme is an attractive antibacterial drug target involved in peptidoglycan synthesis
synthesis
heterologous production of enzyme in Escherichia coli membranes into styrene-maleic acid-wrapped nanodiscs and purification using detergent-free styrene-maleic acid copolymer system. Yield and the purity of the recombinant protein are comparable to enzyme extracted with a conventional detergent. The predominantly alpha-helical secondary structure of the protein in SMA-wrapped nanodiscs is more stable against heat denaturation compared to the micellar protein
synthesis
-
heterologous production of enzyme in Escherichia coli membranes into styrene-maleic acid-wrapped nanodiscs and purification using detergent-free styrene-maleic acid copolymer system. Yield and the purity of the recombinant protein are comparable to enzyme extracted with a conventional detergent. The predominantly alpha-helical secondary structure of the protein in SMA-wrapped nanodiscs is more stable against heat denaturation compared to the micellar protein
-
synthesis
-
the enzyme is an attractive antibacterial drug target involved in peptidoglycan synthesis
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Struve, W.G.; Sinha, R.K.; Neuhaus, F.C.
On the initial stage in peptidoglycan synthesis. Phospho-N-acetylmuramyl-pentapeptide translocase (uridine monophosphate)
Biochemistry
5
82-93
1966
Staphylococcus aureus, Staphylococcus aureus Copenhagen
brenda
Heydanek, M.G.; Neuhaus, F.C.
The initial stage in peptidoglycan synthesis. IV. Solubilization of phospho-N-acetylmuramyl-pentapeptide translocase
Biochemistry
8
1474-1481
1969
Staphylococcus aureus, Staphylococcus aureus Copenhagen
brenda
Umbreit, J.N.; Strominger, J.L.
Complex lipid requirements for detergent-solubilized phosphoacetylmuramyl-pentapeptide translocase from Micrococcus luteus
Proc. Natl. Acad. Sci. USA
69
1972-1974
1972
Micrococcus luteus
brenda
Pless, D.D.; Neuhaus, F.C.
Initial membrane reaction in peptidoglycan synthesis. Lipid dependence of phospho-n-acetylmuramyl-pentapeptide translocase (exchange reaction)
J. Biol. Chem.
248
1568-1576
1973
Staphylococcus aureus, Staphylococcus aureus Copenhagen
brenda
Hammes, W.P.; Neuhaus, F.C.
On the specificity of phospho-N-acetylmuramyl-pentapeptide translocase. The peptide subunit of uridine diphosphate-N-actylmuramyl-pentapeptide
J. Biol. Chem.
249
3140-3150
1974
Staphylococcus aureus, Staphylococcus aureus Copenhagen
brenda
Geis, A.; Plapp, R.
Phospho-N-acetylmuramoyl-pentapeptide-transferase of Escherichia coli K12. Properties of the membrane-bound and the extracted and partially purified enzyme
Biochim. Biophys. Acta
527
414-424
1978
Escherichia coli
brenda
Weppner, W.A.; Neuhaus, F.C.
Initial membrane reaction in peptidoglycan synthesis. Interaction of lipid with phospho-N-acetylmuramyl-pentapeptide translocase
Biochim. Biophys. Acta
552
418-427
1979
Staphylococcus aureus, Staphylococcus aureus Copenhagen
brenda
Tanaka, H.; Oiwa, R.; Matsukura, S.; Inokoshi, J.; Omura, S.
Studies on bacterial cell wall inhibitors. X. Properties of phosph-N-acetylmuramoyl-pentapeptide-transferase in peptidoglycan synthesis of Bacillus megaterium and its inhibition by amphomycin
J. Antibiot.
35
1216-1221
1982
Priestia megaterium, Priestia megaterium KM / ATCC 13632
brenda
Kimura, K.; Miyata, N.; Kawanishi, G.; Kamio, Y.; Izaki, K.; Isono, K.
Liposidomycin C inhibits phospho-N-acetylmuramyl-pentapeptide transferase in peptidoglycan synthesis of Escherichia coli Y-10
Agric. Biol. Chem.
53
1811-1815
1989
Escherichia coli, Escherichia coli Y-10
-
brenda
Ikeda, M.; Wachi, M.; Jung, H.K.; Ishino, F.; Matsuhashi, M.
The Escherichia coli mraY gene encoding UDP-N-acetylmuramoyl-pentapeptide: undecaprenyl-phosphate phospho-N-acetylmuramoyl-pentapeptide transferase
J. Bacteriol.
173
1021-1026
1991
Escherichia coli, Escherichia coli Y-10
brenda
Pickup, K.M.; Bushell, M.E.
Non-fragmenting variants of Streptomyces hyphae have enhanced activity of an enzyme (phospho-N-acetylmuramyl pentapeptide translocase) in peptidoglycan biosynthesis
J. Ferment. Bioeng.
79
247-251
1995
Streptomyces sp.
-
brenda
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
J. Biol. Chem.
271
7609-7614
1996
Escherichia coli, Escherichia coli JM105
brenda
Bouhss, A.; Mengin-Lecreulx, D.; Le Beller, D.; Van Heijenoort, J.
Topological analysis of the MraY protein catalysing the first membrane step of peptidoglycan synthesis
Mol. Microbiol.
34
576-585
1999
Escherichia coli, Staphylococcus aureus
brenda
Azzolina, B.A.; Yuan, X.; Anderson, M.S.; El-Sherbeini, M.
The cell wall and cell division gene cluster in the Mra operon of Pseudomonas aeruginosa: Cloning, production, and purification of active enzymes
Protein Expr. Purif.
21
393-400
2001
Pseudomonas aeruginosa
brenda
Zawadzke, L.E.; Wu, P.; Cook, L.; Fan, L.; Casperson, M.; Kishnani, M.; Calambur, D.; Hofstead, S.J.; Padmanabha, R.
Targeting the MraY and MurG bacterial enzymes for antimicrobial therapeutic intervention
Anal. Biochem.
314
243-252
2003
Escherichia coli
brenda
Stachyra, T.; Dini, C.; Ferrari, P.; Bouhss, A.; Van Heijenoort, J.; Mengin-Lecreulx, D.; Blanot, D.; Biton, J.; Le Beller, D.
Fluorescence detection-based functional assay for high-throughput screening for MraY
Antimicrob. Agents Chemother.
48
897-902
2004
Escherichia coli
brenda
Lloyd, A.J.; Brandish, P.E.; Gilbey, A.M.; Bugg, T.D.H.
Phospho-N-acetyl-muramyl-pentapeptide translocase from Escherichia coli: catalytic role of conserved aspartic acid residues
J. Bacteriol.
186
1747-1757
2004
Escherichia coli
brenda
Bouhss, A.; Crouvoisier, M.; Blanot, D.; Mengin-Lecreulx, D.
Purification and characterization of the bacterial MraY translocase catalyzing the first membrane step of peptidoglycan biosynthesis
J. Biol. Chem.
279
29974-29980
2004
Bacillus subtilis, Escherichia coli, Staphylococcus aureus, Thermotoga maritima
brenda
Schouten, J.A.; Bagga, S.; Lloyd, A.J.; de Pascale, G.; Dowson, C.G.; Roper, D.I.; Bugg, T.D.
Fluorescent reagents for in vitro studies of lipid-linked steps of bacterial peptidoglycan biosynthesis: derivatives of UDPMurNAc-pentapeptide containing d-cysteine at position 4 or 5
Mol. Biosyst.
2
484-491
2006
Escherichia coli, Escherichia coli DH5-alpha
brenda
Mohammadi, T.; Karczmarek, A.; Crouvoisier, M.; Bouhss, A.; Mengin-Lecreulx, D.; den Blaauwen, T.
The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli
Mol. Microbiol.
65
1106-1121
2007
Escherichia coli, Escherichia coli LMC500
brenda
Al-Dabbagh, B.; Henry, X.; El Ghachi, M.; Auger, G.; Blanot, D.; Parquet, C.; Mengin-Lecreulx, D.; Bouhss, A.
Active site mapping of MraY, a member of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase superfamily, catalyzing the first membrane step of peptidoglycan biosynthesis
Biochemistry
47
8919-8928
2008
Bacillus subtilis (Q03521), Bacillus subtilis
brenda
Le Corre, L.; Gravier-Pelletier, C.; Le Merrer, Y.
Towards new MraY inhibitors: a serine template for uracil and 5-amino-5-deoxyribosyl scaffolding
Eur. J. Org. Chem.
2007
5386-5394
2007
Bacteria
-
brenda
Zheng, Y.; Struck, D.K.; Bernhardt, T.G.; Young, R.
Genetic analysis of MraY inhibition by the {varphi}X174 protein E
Genetics
180
1459-1466
2008
Escherichia coli, Bacillus subtilis (Q03521), Bacillus subtilis
brenda
Xu, X.H.; Trunkfield, A.E.; Bugg, T.D.; Qing, F.L.
Synthesis of gem-difluorinated nucleoside analogues of the liposidomycins and evaluation as MraY inhibitors
Org. Biomol. Chem.
6
157-161
2008
Micrococcus flavus
brenda
Kurosu, M.; Mahapatra, S.; Narayanasamy, P.; Crick, D.C.
Chemoenzymatic synthesis of Parks nucleotide: toward the development of high-throughput screening for MraY inhibitors
Tetrahedron Lett.
48
799-803
2007
Bacteria
-
brenda
Murakami, R.; Fujita, Y.; Kizuka, M.; Kagawa, T.; Muramatsu, Y.; Miyakoshi, S.; Takatsu, T.; Inukai, M.
A-94964, a novel inhibitor of bacterial translocase I, produced by Streptomyces sp. SANK 60404. I. Taxonomy, isolation and biological activity
J. Antibiot.
61
537-544
2008
Enterococcus faecalis, Staphylococcus aureus
brenda
Fujita, Y.; Murakami, R.; Muramatsu, Y.; Miyakoshi, S.; Takatsu, T.
A-94964, novel inhibitor of bacterial translocase I, produced by Streptomyces sp. SANK 60404. II. Physico-chemical properties and structure elucidation
J. Antibiot.
61
545-549
2008
Enterococcus faecalis, Staphylococcus aureus
brenda
Shapiro, A.B.; Jahic, H.; Gao, N.; Hajec, L.; Rivin, O.
A high-throughput, homogeneous, fluorescence resonance energy transfer-based assay for phospho-N-acetylmuramoyl-pentapeptide translocase (MraY)
J. Biomol. Screen.
17
662-672
2012
Escherichia coli
brenda
Moberg, A.; Zander Balderud, L.; Hansson, E.; Boyd, H.
Assessing HTS performance using bioassay ontology: screening and analysis of a bacterial phospho-N-acetylmuramoyl-pentapeptide translocase campaign
Assay Drug Dev. Technol.
12
506-513
2014
Bacillus subtilis (Q03521), Bacillus subtilis 168 (Q03521)
brenda
Al-Dabbagh, B.; Olatunji, S.; Crouvoisier, M.; El Ghachi, M.; Blanot, D.; Mengin-Lecreulx, D.; Bouhss, A.
Catalytic mechanism of MraY and WecA, two paralogues of the polyprenyl-phosphate N-acetylhexosamine 1-phosphate transferase superfamily
Biochimie
127
249-257
2016
Bacillus subtilis (Q03521), Bacillus subtilis, Bacillus subtilis 168 (Q03521)
brenda
Ishizaki, Y.; Hayashi, C.; Inoue, K.; Igarashi, M.; Takahashi, Y.; Pujari, V.; Crick, D.C.; Brennan, P.J.; Nomoto, A.
Inhibition of the first step in synthesis of the mycobacterial cell wall core, catalyzed by the GlcNAc-1-phosphate transferase WecA, by the novel caprazamycin derivative CPZEN-45
J. Biol. Chem.
288
30309-30319
2013
Bacillus subtilis (Q03521), Bacillus subtilis, Bacillus subtilis 168 (Q03521)
brenda
Malek Zadeh, S.; Astani, E.K.; Wang, Z.C.; Adhikari, K.; Rattinam, R.; Li, T.L.
Theoretical study of intermolecular interactions between critical residues of membrane protein MraYAA and promising antibiotic muraymycin D2
ACS Omega
5
22739-22749
2020
Aquifex aeolicus (O66465), Aquifex aeolicus
brenda
Yoo, J.; Mashalidis, E.H.; Kuk, A.C.Y.; Yamamoto, K.; Kaeser, B.; Ichikawa, S.; Lee, S.Y.
GlcNAc-1-P-transferase-tunicamycin complex structure reveals basis for inhibition of N-glycosylation
Nat. Struct. Mol. Biol.
25
217-224
2018
Enterocloster bolteae (R0BTE9), Enterocloster bolteae 90A9 (R0BTE9)
brenda
Yamamoto, K.; Sato, T.; Hikiji, Y.; Katsuyama, A.; Matsumaru, T.; Yakushiji, F.; Yokota, S.; Ichikawa, S.
Synthesis and biological evaluation of a MraY selective analogue of tunicamycins
Nucleosides Nucleotides Nucleic Acids
39
349-364
2020
Staphylococcus aureus (R0BTE9), Enterocloster bolteae (R0BTE9), Enterocloster bolteae 90A9 (R0BTE9), Staphylococcus aureus ATCC 25923 (R0BTE9)
brenda
Liu, Y.; Moura, E.C.C.M.; Doerr, J.M.; Scheidelaar, S.; Heger, M.; Egmond, M.R.; Killian, J.A.; Mohammadi, T.; Breukink, E.
Bacillus subtilis MraY in detergent-free system of nanodiscs wrapped by styrene-maleic acid copolymers
PLoS ONE
13
e0206692
2018
Bacillus subtilis (Q03521), Bacillus subtilis 168 (Q03521)
brenda
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EXTERNAL LINKS (specific for EC-Number 2.7.8.13)
Transporter Classification Database (TCDB): 9.B.146.1.3, 9.B.146.1.6
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Release 2023.1 (January 2023)
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