Any feedback?
Information on EC 2.7.8.12 - teichoic acid poly(glycerol phosphate) polymerase
for references in articles please use BRENDA:EC2.7.8.12Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.7.8.12 teichoic acid poly(glycerol phosphate) polymeraseIUBMB Comments
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.
Specify your search results
Word Map
- 2.7.8.12
-
polyglycerol
- epidermidis
- polymerization
-
thermosensitive
-
priming
- polysaccharide
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
n
+
=
n
+
n
+
=
n
+
Synonyms
tagf protein, poly(glycerol phosphate) polymerase, teichoic acid polymerase, cgptase, cdp-glycerol glycerophosphotransferase, glycerophosphate synthetase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CDP-glycerol glycerophosphotransferase
-
-
-
-
CDPglycerol glycerophosphotransferase
-
-
-
-
CDPglycerol:poly(glycerophosphate) glycerophosphotransferase
-
-
-
-
CGPTase
-
-
-
-
glycerophosphate synthetase
-
-
-
-
glycerophosphotransferase, cytidine diphosphoglycerol
-
-
-
-
poly(glycerol phosphate) polymerase
poly(glycerol phosphate)polymerase
TagF protein
teichoic acid glycerol transferase
-
-
-
-
teichoic-acid synthase
-
-
-
-
poly(glycerol phosphate) polymerase
-
-
-
-
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
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
substituted phospho group transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9076-71-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
-
crude extract of protoplast membrane preparation, CMP postulated
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
involved in teichoic acid synthesis
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
-
crude extract of protoplast membrane preparation, CMP postulated
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
-
crude extract of membrane preparation
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
involved in teichoic acid synthesis
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
the enzyme is responsible for the synthesis of wall teichoic acid
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
the enzyme is responsible for the synthesis of wall teichoic acid
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
-
crude extract of membrane preparation
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
involved in teichoic acid synthesis
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
involved in teichoic acid synthesis
-
-
?
additional information
?
-
-
the enzyme plays a role in thermosensitivity
-
-
?
additional information
?
-
-
the enzyme plays a role in thermosensitivity
-
-
?
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
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
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
involved in teichoic acid synthesis
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
involved in teichoic acid synthesis
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
the enzyme is responsible for the synthesis of wall teichoic acid
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
the enzyme is responsible for the synthesis of wall teichoic acid
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
-
involved in teichoic acid synthesis
-
-
?
CDP-glycerol + (glycerophosphate)n
CMP + (glycerophosphate)n+1
involved in teichoic acid synthesis
-
-
?
additional information
?
-
-
the enzyme plays a role in thermosensitivity
-
-
?
additional information
?
-
-
the enzyme plays a role in thermosensitivity
-
-
?
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
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
teichoic acid poly(glycerol phosphate) polymerase deficiency
CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase, which is involved in the synthesis of the major wall teichoic acid in Bacillus subtilis 168, is encoded by tagF (rodC).
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
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 9.5
-
50% of maximal activity at pH 6.5, 25% of maximal activity at pH 8.0, 70% of maximal activity at pH 9.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
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%
Show AA Sequence and Transmembrane Helices (1198 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D630A
-
the ratio of turnover number to KM-value is 3.3fold lower than the wild-type ratio
D645A
-
the ratio of turnover number to KM-value is 3.5fold lower than the wild-type ratio
E604A
-
the ratio of turnover number to KM-value is 1.3fold lower than the wild-type ratio
E639A
-
the ratio of turnover number to KM-value is 3.9fold lower than the wild-type ratio
H474A
-
the ratio of turnover number to KM-value is 4900fold lower than the wild-type ratio
H612A
-
the ratio of turnover number to KM-value is more than 4900fold lower than the wild-type ratio
D630A
-
the ratio of turnover number to KM-value is 3.3fold lower than the wild-type ratio
-
E604A
-
the ratio of turnover number to KM-value is 1.3fold lower than the wild-type ratio
-
E639A
-
the ratio of turnover number to KM-value is 3.9fold lower than the wild-type ratio
-
H474A
-
the ratio of turnover number to KM-value is 4900fold lower than the wild-type ratio
-
H612A
-
the ratio of turnover number to KM-value is more than 4900fold lower than the wild-type ratio
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, the carboxy-terminal His6-tagged TagF protein is stable for several months
-
frozen, no essential loss of activity within several weeks
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
N-terminally truncated construct comprising the catalytic glycerol-phosphate transferase region of the enzyme (residues 312-721) is expressed
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
Burger, M.M.; Glaser, L.
The synthesis of teichoic acids. I. POLYGLYCEROPHOSPHATE
J. Biol. Chem.
239
3168-3177
1964
Bacillus subtilis, Bacillus licheniformis
brenda
Pooley, H.M.; Abellan, F.X.; Karamata, D.
CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase, which is involved in the synthesis of the major wall teichoic acid in Bacillus subtilis 168, is encoded by tagF (rodC)
J. Bacteriol.
1
646-649
1992
Bacillus subtilis, Bacillus subtilis 168
-
brenda
Fitzgerald, S.N.; Foster, T.J.
Molecular analysis of the tagF gene, encoding CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase of Staphylococcus epidermidis ATCC 14990
J. Bacteriol.
182
1046-1052
2000
Staphylococcus epidermidis (Q9RPD1), Staphylococcus epidermidis
brenda
Schertzer, J.W.; Brown, E.D.
Purified, recombinant TagF protein from Bacillus subtilis 168 catalyzes the polymerization of glycerol phosphate onto a membrane acceptor in vitro
J. Biol. Chem.
278
18002-18007
2003
Bacillus subtilis, Bacillus subtilis 168
brenda
Schertzer, J.W.; Bhavsar, A.P.; Brown, E.D.
Two conserved histidine residues are critical to the function of the TagF-like family of enzymes
J. Biol. Chem.
280
36683-36690
2005
Bacillus subtilis, Bacillus subtilis 168
brenda
Lovering, A.L.; Lin, L.Y.; Sewell, E.W.; Spreter, T.; Brown, E.D.; Strynadka, N.C.
Structure of the bacterial teichoic acid polymerase TagF provides insights into membrane association and catalysis
Nat. Struct. Mol. Biol.
17
582-589
2010
Staphylococcus epidermidis (Q5HLM5), Staphylococcus epidermidis
brenda
Tomita, S.; de Waard, P.; Bakx, E.J.; Schols, H.A.; Kleerebezem, M.; Bron, P.A.
The structure of an alternative wall teichoic acid produced by a Lactobacillus plantarum WCFS1 mutant contains a 1,5-linked poly(ribitol phosphate) backbone with 2-alpha-D-glucosyl substitutions
Carbohydr. Res.
370
67-71
2013
Lactiplantibacillus plantarum
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.7.8.12)
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 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
