Any feedback?
No. of entries
Information on EC 2.4.1.227 - undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase
for references in articles please use BRENDA:EC2.4.1.227
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.227 undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase
IUBMB Comments
The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, click here).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
showSynonyms
translocase ii, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylglucosaminyltransferase, uridine diphosphoacetylglucosamine-acetylmuramoylpentapeptide pyrophospholipid
-
-
-
-
gene murG enzyme
-
-
-
-
gene murG proteins
-
-
-
-
Lipid I acetylglucosaminyltransferase
-
-
-
-
MsmegMurG
MurG
MurG glycosyltransferase
-
-
-
-
MurG transferase
peptidoglycan glycosyltransferase
proteins, gene murG
-
-
-
-
UDP-acetylglucosamine-acetylmuramoylpentapeptide pyrophospholipid acetylglucosaminyltransferase
-
-
-
-
UDP-N-acetylglucosamine-N-acetylmuramyl (pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
MurG
-
-
-
-
MurG
-
-
MurG transferase
-
-
-
-
UDP-N-acetylglucosamine-N-acetylmuramyl (pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
-
UDP-N-acetylglucosamine-N-acetylmuramyl (pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-glucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP-N-acetyl-alpha-D-glucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
MurG utilizes an ordered Bi Bi mechanism in which the donor binds first
-
UDP-N-acetyl-alpha-D-glucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
transfer of alpha-N-acetylglucosamine
transfer of alpha-N-acetylglucosamine
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
peptidoglycan biosynthesis I (meso-diaminopimelate containing), peptidoglycan biosynthesis II (staphylococci), peptidoglycan biosynthesis III (mycobacteria), peptidoglycan biosynthesis IV (Enterococcus faecium), peptidoglycan biosynthesis V (beta-lactam resistance)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-glucosamine:N-acetyl-alpha-D-muramyl(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase
The enzyme also works when the lysine residue is replaced by meso-2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined with adjacent residues through its L-centre, as it is in Gram-negative and some Gram-positive organisms. The undecaprenol involved is ditrans,octacis-undecaprenol (for definitions, {iupac/misc/prenol#p6::click here}).
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
60976-26-3
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dUDP-N-acetyl-alpha-D-glucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
?
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + biotinylated citronellyl-lipid I
?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + C55-lipid I-Nepsilon-C6-dansyl thiourea
UDP + C55-lipid II-Nepsilon-C6-dansyl thiourea
UDP-N-acetylglucosamine + biotin-labelled lipid I analogue
?
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + citronellyl-lipid I
UDP + N-acetylglucosamine-citronellyl-lipid I
UDP-N-acetylglucosamine + lipid I
UDP + lipid II
-
Substrates: i.e. Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
Products: i.e. N-acetylglucosamine-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
Products: i.e. N-acetylglucosamine-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-(6E,10E,14Z)-2,6,10,14-tetramethyl-hexadeca-2,6,10,14-tetraene
UDP + GlcNAcbeta(1-4)Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-(6E,10E,14Z)-2,6,10,14-tetramethyl-hexadeca-2,6,10,14-tetraene
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-(7S)-2,7-dimethyloct-2-ene
UDP + GlcNAcbeta(1-4)Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-(7S)-2,7-dimethyloct-2-ene
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-p-nitrophenol
UDP + GlcNAcbeta(1-4)Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-p-nitrophenol
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphobutane
UDP + GlcNAcbeta(1-4)Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphobutane
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphododecane
UDP + GlcNAcbeta(1-4)Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphododecane
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoicosane
UDP + GlcNAcbeta(1-4)Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoicosane
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphotetradecane
UDP + GlcNAcbeta(1-4)Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphotetradecane
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + N-acetylglucosamine-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP-N-acetylglucosamine + MurNAc(Nepsilon-dansylpentapeptide)-pyrophosphoryl (R,S)-alpha-dihydrodecaprenol
UDP + N-acetylglucosamine-MurNAc(Nepsilon-dansylpentapeptide)-pyrophosphoryl (R,S)-alpha-dihydrodecaprenol
-
Substrates: very poor substrate
Products: -
Products: -
?
UDP-N-acetylglucosamine + MurNAc(Nepsilon-dansylpentapeptide)-pyrophosphoryl (R,S)-alpha-dihydroheptaprenol
UDP + N-acetylglucosamine-MurNAc(Nepsilon-dansylpentapeptide)-pyrophosphoryl (R,S)-alpha-dihydroheptaprenol
-
Substrates: -
Products: -
Products: -
r
UDP-N-acetylglucosamine + MurNAc(Neta-dansylpentapeptide)-diphosphoryl (R,S-alpha-dihydroheptaprenol)
?
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + synthetic substrate analogue 2
?
-
Substrates: synthetic substrate analogue 2: a 10 carbon citronellyl derivative
Products: -
Products: -
?
UDP-N-acetylglucosamine + synthetic substrate analogue 7
?
-
Substrates: synthetic substrate analogue 7: a derivative containing a 20 carbon chain with a cis-allylic double bond
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + C55-lipid I-Nepsilon-C6-dansyl thiourea
UDP + C55-lipid II-Nepsilon-C6-dansyl thiourea
A8US35
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + C55-lipid I-Nepsilon-C6-dansyl thiourea
UDP + C55-lipid II-Nepsilon-C6-dansyl thiourea
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetyl-alpha-D-glucosamine + C55-lipid I-Nepsilon-C6-dansyl thiourea
UDP + C55-lipid II-Nepsilon-C6-dansyl thiourea
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + citronellyl-lipid I
UDP + N-acetylglucosamine-citronellyl-lipid I
-
Substrates: undecaprenol replaced with a citronellol group
Products: -
Products: -
?
UDP-N-acetylglucosamine + citronellyl-lipid I
UDP + N-acetylglucosamine-citronellyl-lipid I
-
Substrates: synthetic substrate, 55-carbon undecaprenol chain replaced by the 10-carbon chain of citronellol, biotin labeled substrate
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: lipid I
Products: lipid II
Products: lipid II
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: lipid I
Products: lipid II
Products: lipid II
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + N-acetylglucosamine-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + N-acetylglucosamine-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: sMurG uses UDP-N-acetylglucosamine as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: sMurG uses UDP-N-acetylglucosamine as substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: MurG binds significantly better to UDP than to CDP, ADP or GDP, E269 is an important residue in binding the nucleotide-sugar donor
Products: -
Products: -
?
additional information
?
-
-
Substrates: MurG requires substrates containing an intact amide between the muramyl lactyl ether side-chain and the pentapeptide
Products: -
Products: -
?
additional information
?
-
Substrates: no substrates: TDP-GlcNAc, C4 hydroxyl of UDP-GalNAc cannot form hydrogen bonds to A264 or N292
Products: -
Products: -
?
additional information
?
-
-
Substrates: MurG prefers substrates that contain lipid chains that are considerably shorter than that of the natural substrate, compounds that contain a cis-allylic double bond react faster than compounds that do not
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: P1-citronellyl-P2-alpha-D-glucosyl pyrophosphate, P1-citronellyl-P2-alpha-D-N-acetylglucoseaminyl pyrophosphate, P1-citronellyl-P2-alpha-D-N-acetylmuramyl pyrophosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: role of enzyme in peptidoglycan biosynthesis pathway
Products: -
Products: -
?
additional information
?
-
-
Substrates: UDP-N-acetylgalactosamine shows very little donor activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: UDP-GlcNAc is incorporated into lipid II using GlcNAc. MurG is also able to exchange the GlcNAc of the lipid II head group with GlcNAc of UDPGlcNAc, a simple exchange reaction
Products: -
Products: -
?
additional information
?
-
-
Substrates: UDP-GlcNAc is incorporated into lipid II using GlcNAc. MurG is also able to exchange the GlcNAc of the lipid II head group with GlcNAc of UDPGlcNAc, a simple exchange reaction
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + N-acetylglucosamine-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
additional information
?
-
-
Substrates: role of enzyme in peptidoglycan biosynthesis pathway
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: lipid I
Products: lipid II
Products: lipid II
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: lipid I
Products: lipid II
Products: lipid II
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + N-acetylglucosamine-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: -
Products: -
Products: -
?
UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
UDP + N-acetylglucosamine-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1R,3R,3aS,6aR)-1-{[2-({[(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl] methyl}amino)-2-oxoethyl]carbamoyl}-3-(2-methoxyphenyl)-1-methyl-4,6-dioxo-5-phenyloctahydropyrrolo[3,4-c]pyrrol-2-ium
-
-
(1R,3S,3aR,6aS)-3-((S)-1,2-dihydroxyethyl)-N-(2-((((2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl)methyl)amino)-2-oxoethyl)-1-methyl-4,6-dioxo-5-phenyloctahydropyrrolo[3,4-c]pyrrole-1-carboxamide
-
-
(1R,3S,3aR,6aS)-3-(2,3-dimethoxyphenyl)-N-[2-({[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}amino)-2-oxoethyl]-1-methyl-4,6-dioxo-5-phenyloctahydropyrrolo[3,4-c]pyrrole-1-carboxamide
-
-
(1R,3S,3aR,6aS)-N-[2-({[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}amino)-2-oxoethyl]-1-methyl-4,6-dioxo-3,5-diphenyloctahydropyrrolo[3,4-c]pyrrole-1-carboxamide
-
-
(1R,3S,3aR,6aS)-N-[2-({[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}amino)-2-oxoethyl]-3-(2-methoxyphenyl)-1-methyl-4,6-dioxo-5-phenyloctahydropyrrolo[3,4-c]pyrrole-1-carboxamide
-
-
(1R,3S,3aR,6aS)-N-[2-({[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}amino)-2-oxoethyl]-3-(2-methoxyphenyl)-2-methyl-4,6-dioxo-5-phenyloctahydropyrrolo[3,4-c]pyrrole-1-carboxamide
-
-
(2R)-2-((2S,3S)-2-amino-3-([(2S,3R,4S,5R)-5-(aminomethyl)-3,4-dihydroxyoxolan-2-yl]oxy)-3-[(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxyoxolan-2-yl]propanamido)-3-[([1,1'-biphenyl]-4-carbonyl)oxy]propanoic acid
CHEMBL265692, exhibits very good binding affinity to Mur enzymes: murA, murB, murC, murD, murE, murF, murG and murI, which are involved in peptidoglycan synthesis pathways of Mycobacterium tuberculosis. Identified by molecular docking, MD simulation and binding free energy calculation
(2S)-N-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}-1-{[(1R,3S,3aR,6aS)-3-(2-methoxyphenyl)-1-methyl-4,6-dioxo-5-phenyloctahydropyrrolo[3,4-c]pyrrol-1-yl]carbonyl}pyrrolidine-2-carboxamide
-
-
(2S)-N-{[(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}-1-{[(1R,3S,3aR,6aS)-5-ethyl-3-(2-methoxyphenyl)-1-methyl-4,6-dioxooctahydropyrrolo[3,4-c]pyrrol-1-yl]carbonyl}pyrrolidine-2-carboxamide
-
-
(4R,4aR,5aS,6R,12aS)-4-(dimethylamino)-1,5,10,12,12a-pentahydroxy-6-methyl-3,11-dioxo-3,4,4a,5,5a,6,11,12a- octahydrotetracene-2-carboxamide
-
-
(5E)-5-[(4-tert-butylphenyl)methylidene]-3-[(4-methylpiperidin-1-yl)methyl]-2-sulfanylidene-1,3-thiazolidin-4-one
-
-
(5E)-5-[(5-bromofuran-2-yl)methylidene]-1-(4-chlorophenyl)-1,3-diazinane-2,4,6-trione
-
-
({2-[3-(4-methoxybenzyl)-6-(methoxycarbonyl)-3,4,6,7-tetrahydro-5H-imidazo[4,5-c]pyridin-5-yl]-2-oxoethyl}sulfanyl)acetic acid
-
-
2,2'-disulfanediylbis(N-[2-(3,4-dihydroxyphenyl)-2-hydroxyethyl]benzamide)
CHEMBL296650, exhibits very good binding affinity to Mur enzymes: murA, murB, murC, murD, murE, murF, murG and murI, which are involved in peptidoglycan synthesis pathways of Mycobacterium tuberculosis. Identified by molecular docking, MD simulation and binding free energy calculation
2-alpha-hydroxycostic acid
identified in silico, docking score -8.791 kcal/mol
-
2-[(5Z)-5-(1-benzyl-5-bromo-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]ethane-1-sulfonic acid
-
-
3-[[(3E)-3-[[5-(4-bromophenyl)furan-2-yl]methylidene]-2-oxo-5-phenyl-2,3-dihydro-1H-pyrrol-1-yl]methyl]benzoic acid
-
-
4-{[(1S,11aS)-5,11-dioxo-7-phenyl-2,3,5,10,11,11a-hexahydro-1H-pyrrolo[2,1-c][1,4]benzodiazepin-1-yl]amino}-4-oxobutanoic acid
-
-
5'-({[(2R,3R,3aR,6aR)-3-carboxy-2-(2,3-dihydroxypropyl)-6a-methyl-4,6-dioxohexahydropyrrolo[3,4-b]pyrrol-5(1H)-yl]acetyl}amino)-5'-deoxyuridine
-
-
5'-({[(2S,3R,3aR,6aR)-3-carboxy-2-(2-methoxyphenyl)-6a-methyl-4,6-dioxohexahydropyrrolo[3,4-b]pyrrol-5(1H)-yl]acetyl}amino)-5'-deoxyuridine
-
-
5'-({[(2S,3R,3aS,6aR)-3-carboxy-2-(2,3-dimethoxyphenyl)-6a-methyl-4,6-dioxohexahydropyrrolo[3,4-b]pyrrol-5(1H)-yl]acetyl}amino)-5'-deoxyuridine
-
-
5'-({[(2S,3R,3aS,6aR)-3-carboxy-2-(2-methoxyphenyl)-6a-methyl-4,6-dioxohexahydropyrrolo[3,4-b]pyrrol-5(1H)-yl]acetyl}amino)-5'-deoxyuridine
-
-
5'-({[(2S,3R,3aS,6aR)-3-carboxy-2-(3,4-dimethoxyphenyl)-6a-methyl-4,6-dioxohexahydropyrrolo[3,4-b]pyrrol-5(1H)-yl]acetyl}amino)-5'-deoxyuridine
-
-
5'-({[(2S,3R,3aS,6aR)-3-carboxy-6a-methyl-4,6-dioxo-2-phenylhexahydropyrrolo[3,4-b]pyrrol-5(1H)-yl]acetyl}amino)-5'-deoxyuridine
-
-
5'-deoxy-2-ethyl-5'-(([2-(4-hydroxy-6-methoxy-7-methyl-3-oxo-1,3-dihydro-2-benzofuran-5-yl)ethyl]sulfamoyl)methanesulfonamido)adenosine
CHEMBL444916, exhibits very good binding affinity to Mur enzymes: murA, murB, murC, murD, murE, murF, murG and murI, which are involved in peptidoglycan synthesis pathways of Mycobacterium tuberculosis. Identified by molecular docking, MD simulation and binding free energy calculation
5'-deoxy-5'-[(N-{[(2R,3R,4R,5R)-3-(methoxycarbonyl)-5-(2-methoxyphenyl)-2,4-dimethylpyrrolidinium-2-yl]carbonyl}glycyl) amino]uridine
-
-
5'-O-(3-{[(1R,3S,3aR,6aS)-3-(2-methoxyphenyl)-1-methyl-4,6-dioxo-5-phenyloctahydropyrrolo[3,4-c]pyrrol-1-yl]methoxy}-3-oxopropanoyl)uridine
-
-
5'-O-(4-{[(1R,3S,3aR,6aS)-3-(2-methoxyphenyl)-1-methyl-4,6-dioxo-5-phenyloctahydropyrrolo[3,4-c]pyrrol-1-yl]methoxy}-4-oxobutanoyl)uridine
-
-
5'-[(1-{[(2R,3R,4R,5S)-3,4-bis(methoxycarbonyl)-5-(2-methoxyphenyl)-2-methylpyrrolidin-2-yl]carbonyl}-L-prolyl)amino]-5'-deoxyuridine
-
-
5'-[(1-{[(2R,3S,4R,5S)-3,4-bis(methoxycarbonyl)-5-(2-methoxyphenyl)-2-methylpyrrolidin-2-yl]carbonyl}-L-prolyl)amino]-5'-deoxyuridine
-
-
5'-{[(3S,4R,5S)-3,4-bis(methoxycarbonyl)-5-(2-methoxyphenyl)-2-methyl-D-prolylglycyl]amino}-5'-deoxyuridine
-
-
5'-{[(3S5'-{[(3S,4R,5S)-3,4-bis(methoxycarbonyl)-2-methyl-5-phenyl-D-prolylglycyl]amino}-5'-deoxyuridine,4R,5S)-3,4-bis(methoxycarbonyl)-2-methyl-5-phenyl-D-prolylglycyl]amino}-5'-deoxyuridine
-
-
5-(3-[(E)-[1-(3-chlorophenyl)-2,4,6-trioxo-1,3-diazinan-5-ylidene]methyl]-2,5-dimethyl-1H-pyrrol-1-yl)benzene-1,3-dicarboxylic acid
-
-
5-([3-[2-(4-tert-butylphenoxy)ethoxy]phenyl]methylidene)-2-sulfanylidene-1,3-diazinane-4,6-dione
-
-
aurantiamide
identified in silico, docking score -8.779 kcal/mol
demethoxycurcumin
identified in silico, docking score -8.850 kcal/mol
murgocil
-
a highly bioactive staphylococcal-specific inhibitor of intracellular membrane-associated enzyme MurG
mycothiol bimane
CHEMBL82570, exhibits very good binding affinity to Mur enzymes: murA, murB, murC, murD, murE, murF, murG and murI, which are involved in peptidoglycan synthesis pathways of Mycobacterium tuberculosis. Identified by molecular docking, MD simulation and binding free energy calculation
N-(3-([2-(2,6-dioxopiperidin-3-yl)-1,3-dioxo-2,3-dihydro-1H-isoindol-5-yl]amino)propyl)-2,3,5,6-tetrahydroxy-4-([(2S,3R,4S,5R,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy)hexanamide
CHEMBL446262, exhibits very good binding affinity to Mur enzymes: murA, murB, murC, murD, murE, murF, murG and murI, which are involved in peptidoglycan synthesis pathways of Mycobacterium tuberculosis. Identified by molecular docking, MD simulation and binding free energy calculation. CHEMBL446262 is the top-ranked compound
N-({6-[(4-cyano-2-fluorobenzyl)oxy]naphthalen-2-yl}sulfonyl)-D-glutamic acid
-
-
okaramine I
inhibitor identified in silico, FRED Chemgauss4 score -10.2568
petasiphenol
identified in silico, docking score -8.685 kcal/mol
-
quercetin
binds stably to MurG, forming a strong and stable interaction with potential therapeutic implications. MurG's structural flexibility is reduced upon quercetin binding
Theobromine
identified in silico, docking score -8.881 kcal/mol
Z324718246_1
inhibitor identified in silico, binding affinity -9.9 kcal/mol
Z324718246_2
inhibitor identified in silico, binding affinity -10.2 kcal/mol
Z95813755_1
inhibitor identified in silico, binding affinity -9.9 kcal/mol
[(5E)-5-[(3-bromo-5-chloro-2-hydroxyphenyl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]acetic acid
-
-
UDP
-
competitive inhibitor of UDP-GlcNAc donor, noncompetitive inhibitor of lipid I acceptor analogue
additional information
-
inhibitor binding mode, molecular modeling, overview
-
additional information
-
not inhibited by UMP, nor any other nucleotide diphosphate, UDP-N-acetylgalactosamine fails to show inhibitory activity even at millimolar concentrations
-
additional information
-
a transition state mimic is designed for MurG, containing a functionalised proline, linked through the alpha-carboxylic acid, via a spacer, to a uridine nucleoside. A set of 15 functionalised prolines are synthesised, using a convergent dipolar cycloaddition reaction, which are coupled via either a glycine, proline, sarcosine, or diester linkage to the 5'-position of uridine. The library of 18 final compounds are tested as inhibitors of Escherichia coli glycosyltransferase MurG, overview
-
additional information
molecular docking, MD simulation and binding free energy calculation is employed to identify novel antimycobacterial drug candidates that simultaneously target multiple Mur enzymes of Mycobacterium tuberculosis. Screening of the ChEMBL database
-
additional information
amino acid Arg163 is a key amino acid residue in holding and forming a steady complex of hit phytomolecules through hydrogen bonds and water bridges. Asn124 and Ser244 as well as Ile243 also play important roles in the formation of a stable complex
-
additional information
-
beta-lactam potentiation screening to identify small molecules that augment the activity of beta-lactams against methicillin-resistant Staphylococcus aureus (MRSA), mechanistic characterization of a compound termed murgocil. Chemical synergy and cidality is achieved between murgocil and the beta-lactam imipenem mediated through MurG-dependent localization of penicillin-binding protein PBP2 to the division septum
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cardiolipin
-
the activity of MurG is increased in the presence of cardiolipin
DMSO
-
high concentration (35%) of dimethylsulfoxide is necessary for maximal enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Whooping Cough
The MurG glycosyltransferase provides an oligomeric scaffold for the cytoplasmic steps of peptidoglycan biosynthesis in the human pathogen Bordetella pertussis.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.053
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-(6E,10E,14Z)-2,6,10,14-tetramethyl-hexadeca-2,6,10,14-tetraene
-
pH 7.9, 37°C
0.047
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-(7S)-2,7-dimethyloct-2-ene
-
pH 7.9, 37°C
0.024
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphospho-p-nitrophenol
-
pH 7.9, 37°C
0.022
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphobutane
-
pH 7.9, 37°C
0.029
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphododecane
-
pH 7.9, 37°C
0.052
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoicosane
-
pH 7.9, 37°C
0.039
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphotetradecane
-
pH 7.9, 37°C
0.02
Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
-
pH 7.9, 37°C
0.0028
MurNAc(Nepsilon-dansylpentapeptide)-pyrophosphoryl (R,S)-alpha-dihydroheptaprenol
-
-
0.0028 - 0.011
MurNAc(Neta-dansylpentapeptide)-diphosphoryl (R,S-alpha-dihydroheptaprenol)
additional information
additional information
-
continous fluorescence coupled enzyme assay method
-
0.0028
biotin-labelled lipid I analogue
-
in the presence of high concentration (35%) of dimethylsulfoxide
-
0.044
biotinylated citronellyl-lipid I
-
in the absence of additional metal ions
0.0028
MurNAc(Neta-dansylpentapeptide)-diphosphoryl (R,S-alpha-dihydroheptaprenol)
wild-type enzyme
0.0029
MurNAc(Neta-dansylpentapeptide)-diphosphoryl (R,S-alpha-dihydroheptaprenol)
mutant R260A
0.0042
MurNAc(Neta-dansylpentapeptide)-diphosphoryl (R,S-alpha-dihydroheptaprenol)
mutant N198A
0.0055
MurNAc(Neta-dansylpentapeptide)-diphosphoryl (R,S-alpha-dihydroheptaprenol)
mutant T15A
0.0059
MurNAc(Neta-dansylpentapeptide)-diphosphoryl (R,S-alpha-dihydroheptaprenol)
mutant Y105A
0.0071
MurNAc(Neta-dansylpentapeptide)-diphosphoryl (R,S-alpha-dihydroheptaprenol)
mutant S191A
0.0085
MurNAc(Neta-dansylpentapeptide)-diphosphoryl (R,S-alpha-dihydroheptaprenol)
mutant N291A
0.009
MurNAc(Neta-dansylpentapeptide)-diphosphoryl (R,S-alpha-dihydroheptaprenol)
mutant H124A
0.011
MurNAc(Neta-dansylpentapeptide)-diphosphoryl (R,S-alpha-dihydroheptaprenol)
mutant E125A
0.053
synthetic substrate analogue 7
-
derivative containing a 20 carbon chain with a cis-allylic double bond
-
0.15
UDP-N-acetylglucosamine
-
in the presence of high concentration (35%) of dimethylsulfoxide
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.933
MurNAc(Nepsilon-dansylpentapeptide)-pyrophosphoryl (R,S)-alpha-dihydroheptaprenol
-
-
0.123
biotinylated citronellyl-lipid I
-
in the absence of additional metal ions
14
synthetic substrate analogue 7
-
derivative containing a 20 carbon chain with a cis-allylic double bond
-
0.93
UDP-N-acetylglucosamine
-
in the presence of high concentration (35%) of dimethylsulfoxide
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00249
Z324718246_1
estimated value, pH not specified in the publication, temperature not specified in the publication
0.00234
Z324718246_2
estimated value, pH not specified in the publication, temperature not specified in the publication
0.00239
Z95813755_1
estimated value, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0014
(5E)-5-[(4-tert-butylphenyl)methylidene]-3-[(4-methylpiperidin-1-yl)methyl]-2-sulfanylidene-1,3-thiazolidin-4-one
Escherichia coli
-
pH 7.9, temperature not specified in the publication
0.0064
(5E)-5-[(5-bromofuran-2-yl)methylidene]-1-(4-chlorophenyl)-1,3-diazinane-2,4,6-trione
Escherichia coli
-
pH 7.9, temperature not specified in the publication
0.0035
2-[(5Z)-5-(1-benzyl-5-bromo-2-oxo-1,2-dihydro-3H-indol-3-ylidene)-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]ethane-1-sulfonic acid
Escherichia coli
-
pH 7.9, temperature not specified in the publication
0.0054
3-[[(3E)-3-[[5-(4-bromophenyl)furan-2-yl]methylidene]-2-oxo-5-phenyl-2,3-dihydro-1H-pyrrol-1-yl]methyl]benzoic acid
Escherichia coli
-
pH 7.9, temperature not specified in the publication
0.0014
5-(3-[(E)-[1-(3-chlorophenyl)-2,4,6-trioxo-1,3-diazinan-5-ylidene]methyl]-2,5-dimethyl-1H-pyrrol-1-yl)benzene-1,3-dicarboxylic acid
Escherichia coli
-
pH 7.9, temperature not specified in the publication
0.004
5-([3-[2-(4-tert-butylphenoxy)ethoxy]phenyl]methylidene)-2-sulfanylidene-1,3-diazinane-4,6-dione
Escherichia coli
-
pH 7.9, temperature not specified in the publication
0.0034
[(5E)-5-[(3-bromo-5-chloro-2-hydroxyphenyl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]acetic acid
Escherichia coli
-
pH 7.9, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
enzyme activity is higher in vesicles containing cardiolipin than for vesicles with phosphatidylglycerol
additional information
-
high-throughput method for measurement of enzyme activity based on addititon of UDP[3H]N-acetylglucosamine to membranes in which substrtae lipid I was preformed
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
35
37
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains JM83, JM109, OV2,GS58, RM4102 lysA, OV2 lysA and GS58 lysA
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
during exponential growth, MurG localizes to septa of Bacillus subtilis, a zone of active peptidoglycan synthesis, and its N-terminal amphipathic helix is dispensable
brenda
additional information
-
MurG becomes polarly localized when expressed at high cellular concentrations, only at levels that saturate MurGs cellular requirement for growth, the polar MurG is not active
-
brenda
-
the enzyme localization to the membrane depends on the phospholipid cardiolipin
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
malfunction
-
point mutations in a MurG helical causes severe sporulation defects, but does not affect localization nor cause detectable defects during exponential growth. In strains in which the cardiolipin-synthesizing genes are deleted, MurG levels are diminished at the forespore, but MurG localization during sporulation is rescued by external addition of purified cardiolipin. During sporulation, lack of MurG localization heavily affects engulfment dynamics and sporulation efficiency, indicating a defect in MurG enzymatic activity linked to its diffuse localization
metabolism
physiological function
additional information
drug target
the enzyme is an important and unique drug target in Acinetobacter baumannii since it plays a key role during the synthesis of peptidoglycan and it is not found in Homo sapiens
drug target
identification of novel multitarget antitubercular inhibitors against mycobacterial peptidoglycan biosynthetic Mur enzymes (murA, murB, murC, murD, murE, murF, murG and murI) by structure-based virtual screening
drug target
-
identification of novel multitarget antitubercular inhibitors against mycobacterial peptidoglycan biosynthetic Mur enzymes (murA, murB, murC, murD, murE, murF, murG and murI) by structure-based virtual screening
-
drug target
-
the enzyme is an important and unique drug target in Acinetobacter baumannii since it plays a key role during the synthesis of peptidoglycan and it is not found in Homo sapiens
-
metabolism
-
MurG is an essential N-acetylglucosaminyl transferase involved in catalyzing the final step of peptidoglycan subunit biosynthesis
metabolism
-
glycosyltransferase MurG catalyses the transfer of N-acetyl-D-glucosamine to lipid intermediate I on the bacterial peptidoglycan biosynthesis pathway
metabolism
A8US35
the enzyme is an essential bacterial glycosyltransferase that catalyses the GlcNAc-transformation of lipid I to lipid II during peptidoglycan biosynthesis
metabolism
-
the enzyme is an essential bacterial glycosyltransferase that catalyses the GlcNAc-transformation of lipid I to lipid II during peptidoglycan biosynthesis
metabolism
-
the enzyme is an essential bacterial glycosyltransferase that catalyses the GlcNAc-transformation of lipid I to lipid II during peptidoglycan biosynthesis
-
physiological function
-
MurG represents a temporary storage mechanism for excess protein that can later be remobilized into the active pool. Polar MurG can promote polar accumulation of anionic phospholipids
physiological function
MurG is an essential bacterial glycosyltransferase enzyme in Pseudomonas aeruginosa performing one of the key membrane steps of peptidoglycan synthesis catalyzing the transfer of N-acetyl glucosamine (GlcNAc) from its donor substrate, UDP-GlcNAc, to the acceptor substrate Lipid I
physiological function
-
the glycosyltransferase MurG is necessary for cell wall synthesis at the spore during sporulation in the bacterium Bacillus subtilis. The enzyme localization is a critical factor in the regulation of proper enzyme function and catalysis
physiological function
-
the biochemical production of lipid II requires four components, the lipid carrier undecaprenyl phosphate, UDP-MurNAc-pentapeptide, UDP-GlcNAc and the enzymes catalysing the formation of lipid II from these substrates, MraY and MurG
physiological function
-
the biochemical production of lipid II requires four components, the lipid carrier undecaprenyl phosphate, UDP-MurNAc-pentapeptide, UDP-GlcNAc and the enzymes catalysing the formation of lipid II from these substrates, MraY and MurG
physiological function
the enzyme is involved in peptidoglycan biosynthesis
physiological function
-
MurG interacts with UDP-N-acetylglucosamine 1-carboxyvinyltransferase MurA. MurA adaptive mutant A149E shows a 16fold increase in affinity for MurG. Exposure to daptomycin leads to mislocalization of cell division proteins including MurG. Increasing the stability of MurA-MurG interactions may reduce mislocalization
physiological function
-
the enzyme is involved in peptidoglycan biosynthesis
-
additional information
-
MurG becomes polarly localized when expressed at high cellular concentrations, only at levels that saturate MurGs cellular requirement for growth, the polar MurG is not active and polar MurG is dynamic. It can be remobilized when MurG levels drop
additional information
large-scale conformational change in the relative orientations of the N- and C-terminal domains, which has the effect of widening the cofactor binding site and displacing the UDP-GlcNAc donor
additional information
-
docking of transition state analogues into MurG active site, overview
additional information
-
the active site residue Gln298 plays a critical role in ligand-target interactions, other active site residues like Arg168, Ser198, Arg202, Ser269, and His297 also play roles in binding interactions, docking study, and molecular modeling and structure validation, overview
additional information
-
the active site residue Gln298 plays a critical role in ligand-target interactions, other active site residues like Arg168, Ser198, Arg202, Ser269, and His297 also play roles in binding interactions, docking study, and molecular modeling and structure validation, overview
-
Show AA Sequence and Transmembrane Helices (20027 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37800
38000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
structure comparison with the enzyme from Escherichia coli, molecular modeling and structure validation, overview
additional information
-
structure comparison with the enzyme from Escherichia coli, molecular modeling and structure validation, overview
-
additional information
structure comparison with the MurG enzyme from Escherichia coli, overview
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex of MurG with UDP-GlcNAc, X-ray diffraction structure determination and analysis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F77E
-
site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type. Lipid II synthesis might be totally abrogated in mutant F77E explaining why the mutant is blocked in septation, cell wall synthesis is necessary for engulfment
S67E
-
site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type
V74E
-
site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type. Lipid II synthesis might be totally abrogated in mutant V74E explaining why the mutant is blocked in septation, cell wall synthesis is necessary for engulfment
V81E
-
site-directed mutagenesis, the mutant shows unaltered localization and cell growth comared to wild-type
E125A
amino acid substitution for evaluation of its role in the active site of MurG
E268A
H124A
amino acid substitution for evaluation of its role in the active site of MurG
H18A
amino acid substitution for evaluation of its role in the active site of MurG
L79E/F82E
-
site-directed mutagenesis, the mutant does not bind anionic phospholipids but can localize to the cell poles
N127A
amino acid substitution for evaluation of its role in the active site of MurG
N134A
amino acid substitution for evaluation of its role in the active site of MurG
N198A
amino acid substitution for evaluation of its role in the active site of MurG
N291A
amino acid substitution for evaluation of its role in the active site of MurG
Q288A
amino acid substitution for evaluation of its role in the active site of MurG
R260A
amino acid substitution for evaluation of its role in the active site of MurG
S191A
amino acid substitution for evaluation of its role in the active site of MurG
T15A
amino acid substitution for evaluation of its role in the active site of MurG
Y105A
amino acid substitution for evaluation of its role in the active site of MurG
additional information
-
none of the point mutations shows lethality and cells expressing MurG-GFP point mutants grow normally in absence of the wild-type murG allele
E268A
amino acid substitution for evaluation of its role in the active site of MurG
E268A
-
site-directed mutagenesis, in contrast to wild-type MurG, the MurG lipid interaction mutant often localizes to a single pole
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native MurG is extracted from inner membrane vesicles of Escherichia coli cells, His-tagged MurG is purified by Ni-affinity chromatography using His-bind resin
-
recombinant His6-tagged enzyme from Escherichia coli strain C43 by nickel affinity chromatography
-
when overexpressed, enzyme copurifies with lipid vesicles deriving from intracellular vesicular mebranes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli cells BL21-DE3-pLysS
gene murG, expression as His6-tagged enzyme in Escherichia coli strain C43
-
gene murG, expression of C-terminal YFP-tagged enzyme in a murG-deficient strain of Bacillus subtilis
-
into the vector pQE60 for expression of MurG in Escherichia coli JM109 cells
MurG can be displayed in its active form on phage. Cloned from a pET-21a expression vector (Novagen) into the pFAB5cHis.TT.HUI phagemid vector as a fusion to the 3-end of a pelB leader sequence and the 5-end of a truncated gIII
-
the coding sequence is amplified from the Escherichia coli K12 chromosome and cloned for expression of His-tagged MurG in JM109 cells
-
the murG gene is cloned with an N-terminal His6 tag into a pET33b vector. The plasmid is transformed and expressed in Escherichia coli NiCo21(DE3) competent cells
-
the murG gene is cloned with an N-terminal His6 tag into a pET33b vector. The plasmid was transformed and expressed in Escherichia coli NiCo21(DE3) competent cells
A8US35
expressed in Escherichia coli cells BL21-DE3-pLysS
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
drug development
synthesis
-
overexpression of enzyme results in formation of vesicular intracellular membranes enriched in cardiolipin. Cardiolipin content of cell is about 7fold increased
biotechnology
-
MurG is interesting to evaluate as a potential antibiotic target, as it has no counterpart in mammalian cells
biotechnology
-
MurG is interesting to evaluate as a potential antibiotic target, as it has no counterpart in mammalian cells
-
drug development
-
MurG is a target for drug development to treat diseases caused by Clostridium difficile, an etiologic agent of a variety of gastrointestinal diseases in humans including mild sporadic diarrhea and severe life-threatening pseudomembranous colitis
drug development
the enzyme is an important and unique drug target in Acinetobacter baumannii since it plays a key role during the synthesis of peptidoglycan and it is not found in Homo sapiens. In-silico based exploring of potential lead candidates from the library of natural products for the treatment of Acinetobacter baumannii infections is accomplished with the aid of systematic computational analysis. A 3D model of MurG is predicted using comparative protein modeling approach based on homologous MurG structure from Escherichia coli (strain K12) (PDB ID: 1F0K). Concordance binding site analysis is performed to identify the putative ligand binding sites of optimized MurG model for virtual screening and docking studies against natural compounds subset of Zinc database
drug development
-
MurG is a target for drug development to treat diseases caused by Clostridium difficile, an etiologic agent of a variety of gastrointestinal diseases in humans including mild sporadic diarrhea and severe life-threatening pseudomembranous colitis
-
drug development
-
the enzyme is an important and unique drug target in Acinetobacter baumannii since it plays a key role during the synthesis of peptidoglycan and it is not found in Homo sapiens. In-silico based exploring of potential lead candidates from the library of natural products for the treatment of Acinetobacter baumannii infections is accomplished with the aid of systematic computational analysis. A 3D model of MurG is predicted using comparative protein modeling approach based on homologous MurG structure from Escherichia coli (strain K12) (PDB ID: 1F0K). Concordance binding site analysis is performed to identify the putative ligand binding sites of optimized MurG model for virtual screening and docking studies against natural compounds subset of Zinc database
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mengin-Lecreulx, D.; Textier, L.; Rousseau, M.; van Heijenoort, J.
The murG gene of Escherichia coli codes for the UDP-N-acetylglucosamine:N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase involved in the membrane steps of peptidoglycan synthesis
J. Bacteriol.
173
4625-4636
1991
Escherichia coli
brenda
Ha, S.; Chang, E.; Lo, M.C.; Men, H.; Park, P.; Ge, M.; Walker, S.
The kinetik characterization of Escherichia coli MurG using synthetic substrate analogues
J. Am. Chem. Soc.
121
84158426
1999
Escherichia coli
-
brenda
Branstrom, A.A.; Midha, S.; Longley, C.B.; Han, K.; Baizman, E.R.; Axelrod, H.R.
Assay for identification of inhibitors for bacterial MraY translocase or MurG transferase
Anal. Biochem.
280
315-319
2000
Escherichia coli, Escherichia coli OV58-pUG18
brenda
Cudic, P.; Behenna, D.C.; Yu, M.K.; Kruger, R.G.; Szewczuk, L.M.; McCafferty, D.G.
Synthesis of P1-citronellyl-P2-alpha-D-pyranosyl pyrophosphates as potential substrates for the E. coli undecaprenyl-pyrophosphoryl-N-acetylglucoseaminyl transferase MurG
Bioorg. Med. chem. Lett.
11
3107-3110
2001
Escherichia coli
brenda
Men, H.; Park, P.; Walker, S.
Substrate synthesis and activity assay for MurG
J. Am. Chem. Soc.
120
2484-2485
1998
Escherichia coli
-
brenda
Ha, S.; Gross.B.; Walker, S.
E. coli MurG: A paradigm for a superfamily of glycosyltransferases
Curr. Drug Targets Infect. Disord.
1
201-213
2001
Escherichia coli
brenda
Chen, L.; Men, H.; Ha, S.; Ye, X.Y.; Brunner, L.; Hu, Y.; Walker, S.
Intrinsic lipid preferences and kinetic mechanism of Escherichia coli MuG
Biochemistry
41
6824-6833
2002
Escherichia coli
brenda
Hu, Y.; Chen, L.; Ha, S.; Gross, B.; Falcone, B.; Walker, D.; Mokhtarzadeh, M.; Walker, S.
Crystal structure of the MurG: UDP-GlcNAc complex reveals common structural principles of a superfamily of glycosyltransferases
Proc. Natl. Acad. Sci. USA
100
845-849
2003
Escherichia coli (P17443)
brenda
Auger, G.; van Heijenoort, J.; Mengin-Lecreulx, D.; Blanot, D.
A MurG assay which utilises a synthetic analogue of lipid I
FEMS Microbiol. Lett.
219
115-119
2003
Escherichia coli
brenda
Ravishankar, S.; Kumar, V.P.; Chandrakala, B.; Jha, R.K.; Solapure, S.M.; De Sousa, S.M.
Scintillation proximity assay for inhibitors of Escherichia coli MurG and, optionally, MraY
Antimicrob. Agents Chemother.
49
1410-1418
2005
Escherichia coli
brenda
Liu, H.; Ritter, T.K.; Sadamoto, R.; Sears, P.S.; Wu, M.; Wong, C.H.
Acceptor specificity and inhibition of the bacterial cell-wall glycosyltransferase MurG
Chembiochem
4
603-609
2003
Escherichia coli
brenda
van den Brink-van der Laan, E.; Boots, J.W.P.; Spelbrink, R.E.J.; Kool, G.M.; Breukink, E.; Killian, J.A.; de Kruijff, B.
Membrane interaction of the glycosyltransferase MurG: A special role for cardiolipin
J. Bacteriol.
185
3773-3779
2003
Escherichia coli
brenda
Love, K.R.; Swoboda, J.G.; Noren, C.J.; Walker, S.
Enabling glycosyltransferase evolution: a facile substrate-attachment strategy for phage-display enzyme evolution
Chembiochem
7
753-756
2006
Escherichia coli
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
brenda
Crouvoisier, M.; Auger, G.; Blanot, D.; Mengin-Lecreulx, D.
Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis
Biochimie
89
1498-1508
2007
Escherichia coli (P17443)
brenda
Bouhss, A.; Trunkfield, A.; Bugg, T.; Mengin-Lecreulx, D.
The biosynthesis of peptidoglycan lipid-linked intermediates
FEMS Microbiol. Rev.
32
208-233
2008
Escherichia coli
brenda
Trunkfield, A.E.; Gurcha, S.S.; Besra, G.S.; Bugg, T.D.
Inhibition of Escherichia coli glycosyltransferase MurG and Mycobacterium tuberculosis Gal transferase by uridine-linked transition state mimics
Bioorg. Med. Chem.
18
2651-2663
2010
Escherichia coli
brenda
Michaelis, A.M.; Gitai, Z.
Dynamic polar sequestration of excess MurG may regulate enzymatic function
J. Bacteriol.
192
4597-4605
2010
Escherichia coli
brenda
Ezhilarasan, V.; Sharma, O.; Pan, A.
In silico identification of potential drug targets in Clostridium difficile R20291: modeling and virtual screening analysis of a candidate enzyme MurG
Med. Chem. Res.
22
2692-2705
2012
Clostridioides difficile, Clostridioides difficile R20291
-
brenda
Brown, K.; Vial, S.C.; Dedi, N.; Westcott, J.; Scally, S.; Bugg, T.D.; Charlton, P.A.; Cheetham, G.M.
Crystal structure of the Pseudomonas aeruginosa MurG:UDP-GlcNAc substrate complex
Protein Pept. Lett.
20
1002-1008
2013
Pseudomonas aeruginosa (Q9HW01)
brenda
Mann, P.A.; Mueller, A.; Xiao, L.; Pereira, P.M.; Yang, C.; Ho Lee, S.; Wang, H.; Trzeciak, J.; Schneeweis, J.; Dos Santos, M.M.; Murgolo, N.; She, X.; Gill, C.; Balibar, C.J.; Labroli, M.; Su, J.; Flattery, A.; Sherborne, B.; Maier, R.; Tan, C.M.; Black, T.; Onder, K.; Kargman, S.; Monsma, F.J.; Pinho, M.G.; Schneider, T.; Roemer, T.
Murgocil is a highly bioactive staphylococcal-specific inhibitor of the peptidoglycan glycosyltransferase enzyme MurG
ACS Chem. Biol.
8
2442-2451
2013
Staphylococcus aureus
brenda
Gifford, S.M.; Meyer, P.
Enzyme function is regulated by its localization
Comput. Biol. Chem.
59 Pt B
113-122
2015
Bacillus subtilis
brenda
Egan, A.J.; Biboy, J.; vant Veer, I.; Breukink, E.; Vollmer, W.
Activities and regulation of peptidoglycan synthases
Philos. Trans. R. Soc. Lond. B Biol. Sci.
370
20150031
2015
Escherichia coli, Micrococcus flavus
brenda
Mitachi, K.; Yun, H.; Gillman, C.; Skorupinska-Tudek, K.; Swiezewska, E.; Clemons, W.; Kurosu, M.
Substrate tolerance of bacterial glycosyltransferase MurG novel fluorescence-based assays
ACS Infect. Dis.
6
1501-1516
2019
Hydrogenivirga sp. 128-5-R1-1 (A8US35), Mycolicibacterium smegmatis, Mycolicibacterium smegmatis ATCC 607
brenda
Nishimoto, M.
Large scale production of lacto-N-biose I, a building block of type I human milk oligosaccharides, using sugar phosphorylases
Biosci. Biotechnol. Biochem.
84
17-24
2020
Escherichia coli
brenda
Amera, G.M.; Khan, R.J.; Pathak, A.; Jha, R.K.; Muthukumaran, J.; Singh, A.K.
Screening of promising molecules against MurG as drug target in multi-drug-resistant-Acinetobacter baumannii - insights from comparative protein modeling, molecular docking and molecular dynamics simulation
J. Biomol. Struct. Dyn.
2019
1-23
2019
Acinetobacter baumannii (B0V9F5), Acinetobacter baumannii AYE (B0V9F5)
brenda
Kumari, M.; Subbarao, N.
Identification of novel multitarget antitubercular inhibitors against mycobacterial peptidoglycan biosynthetic Mur enzymes by structure-based virtual screening
J. Biomol. Struct. Dyn.
40
8185-8196
2022
Mycobacterium tuberculosis (P9WJK9), Mycobacterium tuberculosis ATCC 25618 (P9WJK9)
brenda
Zhou, Y.; Utama, B.; Pratap, S.; Supandy, A.; Song, X.; Tran, T.T.; Mehta, H.H.; Arias, C.A.; Shamoo, Y.
Enolpyruvate transferase MurAAA149E, identified during adaptation of Enterococcus faecium to daptomycin, increases stability of MurAA-MurG interaction
J. Biol. Chem.
299
102912
2023
Enterococcus faecium
brenda
Lokhande, K.B.; Pawar, S.V.; Madkaiker, S.; Shrivastava, A.; Venkateswara, S.K.; Nawani, N.; Wani, M.; Ghosh, P.; Singh, A.
Screening of potential phytomolecules against MurG as drug target in nosocomial pathogen Pseudomonas aeruginosa perceptions from computational campaign
J. Biomol. Struct. Dyn.
42
495-508
2024
Pseudomonas aeruginosa (Q9HW01), Pseudomonas aeruginosa DSM 22644 (Q9HW01)
brenda
Mahur, P.; Singh, A.K.; Muthukumaran, J.; Jain, M.
Targeting MurG enzyme in Klebsiella pneumoniae An in silico approach to novel antimicrobial discovery
Res. Microbiol.
176
104257
2025
Klebsiella pneumoniae subsp. pneumoniae (A6T4N3), Klebsiella pneumoniae subsp. pneumoniae ATCC 700721 (A6T4N3)
brenda
Shtaiwi, A.; Khan, S.U.; Khedraoui, M.; Alaraj, M.; Samadi, A.; Chtita, S.
A comprehensive computational study to explore promising natural bioactive compounds targeting glycosyltransferase MurG in Escherichia coli for potential drug development
Sci. Rep.
14
7098
2024
Escherichia coli (P17443)
brenda
Goswami, D.; Prajapati, J.; Dabhi, M.; Sharkey, L.K.R.; Pidot, S.J.
MurG as a potential target of quercetin in Staphylococcus aureus supported by evidence from subtractive proteomics and molecular dynamics
Sci. Rep.
15
7309
2025
Staphylococcus aureus (Q6GGZ0), Staphylococcus aureus MRSA252 (Q6GGZ0)
brenda
EXTERNAL LINKS (specific for EC-Number 2.4.1.227)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
