Information on EC 2.7.8.12 - teichoic acid poly(glycerol phosphate) polymerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.8.12
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RECOMMENDED NAME
GeneOntology No.
teichoic acid poly(glycerol phosphate) polymerase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
n CDP-glycerol + 4-O-[(2R)-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol = n CMP + 4-O-{poly[(2R)-glycerophospho]-(2R)-glycerophospho}-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
substituted phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
poly(glycerol phosphate) wall teichoic acid biosynthesis
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teichoic acid biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
CDP-glycerol:4-O-[(2R)-glycerophospho]-N-acetyl-beta-D-mannosaminyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-diphospho-ditrans,octacis-undecaprenol glycerophosphotransferase
Involved in the biosynthesis of poly glycerol phosphate teichoic acids in bacterial cell walls. This enzyme adds 30--50 glycerol units to the linker molecule, but only after it has been primed with the first glycerol unit by EC 2.7.8.44, teichoic acid poly(glycerol phosphate) primase. cf. EC 2.7.8.45, teichoic acid glycerol-phosphate transferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9076-71-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 9945
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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a tagF1-tagF2 deletion mutant of Lactobacillus plantarum, strain WCFS1, lacks poly(glycerol phosphate) polymerase activity required for glycerol-type wall teichoic acid biosynthesis. The mutant activates an alternative genetic locus, tarIJKL, encoding the enzymes for nucleotide activation and incorporation of ribitol in the wall teichoic acid backbone polymer, structure analysis of the alternative ribitol-type wall teichoic acid backbone by HPAEC, UPLC-mass spectrometry, NMR spectroscopy, and MALDI-TOF mass spectrometry, overview, revealing a 1,5-linked poly(ribitol phosphate) which is substituted at the C-2 hydroxyl group of the ribitol residue with alpha-D-glucosyl at a frequency of 28%
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
show the reaction diagram
CDP-glycerol + membrane acceptor
CMP + ?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
show the reaction diagram
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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0.01 M: optimal, requirement for a divalent cation
Mg2+
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0.04 M: optimal, requirement for a divalent cation
Mn2+
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slight stimulation, in presence of Mg2+ inhibition
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bacitracin
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94% of maximal activity
Cetylpyridinium chloride
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47% of maximal activity
Crystal violet
CTP
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excess concentration causes slight inhibition
Mn2+
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slight stimulation, in presence of Mg2+ inhibition
novobiocin
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complete inhibition
penicillin
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27% of maximal activity
Ristocetin
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90% of maximal activity
spermidine
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78% of maximal activity
streptomycin
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89% of maximal activity
Vancomycin
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31% of maximal activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.23 - 0.75
CDP-glycerol
0.00083
CDPglycerol
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12 - 0.233
CDP-glycerol
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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and pH 9.0, 2 maxima
9
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and pH 7.0, 2 maxima
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.5
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50% of maximal activity at pH 6.5, 25% of maximal activity at pH 8.0, 70% of maximal activity at pH 9.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90400
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x * 90400, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure of Staphylococcus epidermidis TagF is determined to 2.7 A resolution from a construct that includes both the membrane-targeting region and the glycerol-phosphate polymerase domains. TagF possesses a helical region for interaction with the lipid bilayer, placing the active site at a suitable distance for access to the membrane-bound substrate
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, little loss of activity after 6 months
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-80°C, 20% glycerol, stable for several months
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-80°C, the carboxy-terminal His6-tagged TagF protein is stable for several months
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frozen, no essential loss of activity within several weeks
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATCC 6051, partial; NCTC 3610, partial
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ATCC 9945, partial
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fusion protein with glutathione S-transferase
recombinant enzyme
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strain 168, partial
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
fusion protein with glutathione S-transferase
N-terminally truncated construct comprising the catalytic glycerol-phosphate transferase region of the enzyme (residues 312-721) is expressed
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D630A
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the ratio of turnover number to KM-value is 3.3fold lower than the wild-type ratio
D645A
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the ratio of turnover number to KM-value is 3.5fold lower than the wild-type ratio
E604A
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the ratio of turnover number to KM-value is 1.3fold lower than the wild-type ratio
E639A
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the ratio of turnover number to KM-value is 3.9fold lower than the wild-type ratio
H474A
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the ratio of turnover number to KM-value is 4900fold lower than the wild-type ratio
H612A
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the ratio of turnover number to KM-value is more than 4900fold lower than the wild-type ratio
D630A
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the ratio of turnover number to KM-value is 3.3fold lower than the wild-type ratio
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E604A
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the ratio of turnover number to KM-value is 1.3fold lower than the wild-type ratio
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E639A
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the ratio of turnover number to KM-value is 3.9fold lower than the wild-type ratio
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H474A
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the ratio of turnover number to KM-value is 4900fold lower than the wild-type ratio
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H612A
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the ratio of turnover number to KM-value is more than 4900fold lower than the wild-type ratio
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DELTA 312-721
truncated construct contains membrane binding region, truncated construct shows same activity as full-length wild-type
H444N
mutant crystallizes identical to wild-type, mutant shows no detectable activity compared to wild-type
H584A
mutant crystallizes identical to wild-type, mutant shows no detectable activity compared to wild-type
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