Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.4.1.129 - peptidoglycan glycosyltransferase and Organism(s) Aquifex aeolicus and UniProt Accession O66874

for references in articles please use BRENDA:EC2.4.1.129
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
                2.4.1.129 peptidoglycan glycosyltransferase
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). Involved in the synthesis of cell-wall peptidoglycan.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Aquifex aeolicus
UNIPROT: O66874
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Aquifex aeolicus
The enzyme appears in selected viruses and cellular organisms
Synonyms
pbp2a, pbp2b, penicillin binding protein, gtase, penicillin-binding protein 3, penicillin-binding protein 2, pbp 2b, pbp 1a, pbp 2x, spoiid, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)-pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D-glucosaminyltransferase
-
-
-
-
glycosyltransferase, peptidoglycan
-
-
-
-
PBP1a
PBP1b
-
-
-
-
penicillin-binding protein 1B
-
-
-
-
penicillin-binding protein 3
-
-
-
-
peptidoglycan transglycosylase
-
-
-
-
PG-II
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
[poly-N-acetyl-D-glucosaminyl-(1->4)-(N-acetyl-D-muramoylpentapeptide)]-diphosphoundecaprenol:[N-acetyl-D-glucosaminyl-(1->4)-N-acetyl-D-muramoylpentapeptide]-diphosphoundecaprenol disaccharidetransferase
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). Involved in the synthesis of cell-wall peptidoglycan.
CAS REGISTRY NUMBER
COMMENTARY hide
79079-04-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
show the reaction diagram
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
show the reaction diagram
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-(L)-meso-diaminopimelic acid-(L)-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
show the reaction diagram
-
-
-
-
?
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n-diphosphoundecaprenol + GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol
[GlcNAc-(1-4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)]n+1-diphosphoundecaprenol + undecaprenyl diphosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
while isoform PBP1a is able to convert lipid IV (heptaprenyl-tetrasaccharide) to peptidoglycan in the absence of lipid II, isoform PBP1b does not use lipid IV as substrate unless lipid II is also present
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
moenomycin A
active site inhibitor
neryl-moenomycin A
active site inhibitor
(3E,7E,14E)-4,9,9,15,19-pentamethyl-12-methylideneicosa-3,7,14,18-tetraen-1-yl (2R)-3-[[[[(2R,3R,4S,5S,6S)-6-carbamoyl-3-[[(2S,3R,4R,5S,6R)-4,5-dihydroxy-6-(hydroxymethyl)-3-([[3-(trifluoromethyl)phenyl]carbonyl]amino)tetrahydro-2H-pyran-2-yl]oxy]-5-hydroxy-4-([[4-(trifluoromethoxy)-3-(trifluoromethyl)phenyl]carbamoyl]amino)tetrahydro-2H-pyran-2-yl]oxy](hydroxy)phosphoryl]oxy]-2-hydroxypropanoate
-
-
(3Z)-5-(4-bromophenyl)-3-[(5-nitrofuran-2-yl)methylidene]furan-2(3H)-one
-
-
(4Z)-2,5-diphenyl-4-[2-(1,3-thiazol-2-yl)hydrazinylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
4-[(1E)-2-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydronaphthalen-2-yl)prop-1-en-1-yl]benzoic acid
-
-
AC326-alpha
-
-
ACL19273
-
-
chlorobiphenyl desleucyl vancomycin
-
-
chlorobiphenyl disaccharide
-
-
chlorobiphenyl vancomycin
-
-
Garneau-5
-
-
moenomycin A
-
-
moenomycin disaccharide
-
-
moenomycin trisaccharide
-
-
TS30153
-
-
Vancomycin
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00388
chlorobiphenyl desleucyl vancomycin
Aquifex aeolicus
-
-
0.0015
chlorobiphenyl vancomycin
Aquifex aeolicus
-
-
0.000006
moenomycin A
Aquifex aeolicus
-
-
0.000033
moenomycin disaccharide
Aquifex aeolicus
-
-
0.000016
moenomycin trisaccharide
Aquifex aeolicus
-
-
0.00038
Vancomycin
Aquifex aeolicus
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
PGT catalyzes the polymerization of lipid II to form the bacterial cell wall
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
complex of neryl-moenomycin A bound to the peptidoglycan glycosyltransferase domain of PBP1A
hanging-drop vapor-diffusion method. 2.1 A crystal structure of the peptidoglycan glycosyltransferase domain of PBP1A along with biochemical studies suggest a model for processive glycosyltransfer
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E83A
mutant with undetectable activity
K124A
mutant shows 5fold reduced activity compared to the wild type enzyme
K137A
mutant with undetectable activity
Q121A
mutant with undetectable activity
R132A
mutant with barely detectable activity (about 3% of wild type)
S116A
mutant shows 10fold reduced activity compared to the wild type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yuan, Y.; Barrett, D.; Zhang, Y.; Kahne, D.; Sliz, P.; Walker, S.
Crystal structure of a peptidoglycan glycosyltransferase suggests a model for processive glycan chain synthesis
Proc. Natl. Acad. Sci. USA
104
5348-5353
2007
Aquifex aeolicus
Manually annotated by BRENDA team
Yuan, Y.; Fuse, S.; Ostash, B.; Sliz, P.; Kahne, D.; Walker, S.
Structural analysis of the contacts anchoring moenomycin to peptidoglycan glycosyltransferases and implications for antibiotic design
ACS Chem. Biol.
3
429-436
2008
Aquifex aeolicus (O66874)
Manually annotated by BRENDA team
Terrak, M.
Peptidoglycan glycosyltransferase inhibition: New perspectives for an old target
Anti-Infect. Agents Med. Chem.
7
180-192
2008
Aquifex aeolicus, Escherichia coli, Enterococcus faecalis, Helicobacter pylori, Staphylococcus aureus, Escherichia coli BAS849
-
Manually annotated by BRENDA team
Lovering, A.L.; Gretes, M.; Strynadka, N.C.
Structural details of the glycosyltransferase step of peptidoglycan assembly
Curr. Opin. Struct. Biol.
18
534-543
2008
Aquifex aeolicus, Bacillus subtilis, Caulobacter vibrioides, Escherichia coli, Staphylococcus aureus, Mycobacterium tuberculosis, Cereibacter sphaeroides
Manually annotated by BRENDA team
Perlstein, D.; Wang, T.; Doud, E.; Kahne, D.; Walker, S.
The role of the substrate lipid in processive glycan polymerization by the peptidoglycan glycosyltransferases
J. Am. Chem. Soc.
132
48-49
2010
Aquifex aeolicus
Manually annotated by BRENDA team