Information on EC 2.7.8.6 - undecaprenyl-phosphate galactose phosphotransferase

for references in articles please use BRENDA:EC2.7.8.6
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.8.6
-
RECOMMENDED NAME
GeneOntology No.
undecaprenyl-phosphate galactose phosphotransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + undecaprenyl phosphate = UMP + alpha-D-galactosyl-diphosphoundecaprenol
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
substituted phospho group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:undecaprenyl-phosphate galactose phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
37278-29-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose + undecaprenyl phosphate
UMP + alpha-D-galactosyl-diphosphoundecaprenol
show the reaction diagram
UDP-D-galactose + antigen carrier lipid-phosphate
UMP + galactose-diphosphate antigen carrier lipid
show the reaction diagram
Salmonella newington
-
-
polyisoprenoid structure linked to sugars by a diphosphate bridge
?
UDP-D-galactose + phosphoryl-polyprenol
galactosyl-diphospho-polyprenol + CMP
show the reaction diagram
UDP-D-N-acetylhexosamine + undecaprenyl phosphate
UMP + N-acetyl hexosaminyl-diphosphoundecaprenol
show the reaction diagram
UDP-galactose + phosphoryl-polyprenol
UMP + alpha-D-galactosyl-diphosphopolyprenol
show the reaction diagram
UDP-N-acetyl-D-galactosamine + undecaprenyl phosphate
UMP + N-acetyl-D-galactosaminyl-diphosphoundecaprenol
show the reaction diagram
UDPgalactose + phospholipid
UMP + galactose-1-diphospho-lipid
show the reaction diagram
additional information
?
-
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
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
without adding MgCl2, no activity can be detected. Activity is optimal at 25 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CHAPS
-
62.4% relative activity at 0.5 mM
dUMP
-
0.13 mM: 48% inhibition, 0.37 mM: 78% inhibition, 1 mM: 87% inhibition
KCl
-
KCl inhibits the enzyme domain activity, particularly at concentrations higher than 200 mM salt that result in more than 50% inhibition
Mg2+
-
no activity at 150 mM
n-dodecyl-beta-D-maltoside
-
81.5% relative activity at 0.5 mM
NaCl
-
NaCl inhibits the enzyme domain activity, particularly at concentrations higher than 200 mM salt that result in more than 50% inhibition
octylglucoside
-
65.5% relative activity at 0.5 mM
UDP
-
0.12 mM: no inhibition, 1 mM: 40% inhibition
UMP
-
0.04 mM: 56% inhibition, 0.1 mM: 76% inhibition, 0.4 mM: 93% inhibition
UTP
-
0.11 mM: 5% inhibition, 1 mM: 49% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00055
UDP-alpha-D-galactose
-
in 50 mM Tris-HCl (pH 8.5), 25 mM MgCl2, 1% (w/v) CHAPS, at 37C
0.0785
undecaprenyl phosphate
-
in 50 mM Tris-HCl (pH 8.5), 25 mM MgCl2, 1% (w/v) CHAPS, at 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
x * 29000, His6-tagged catalytic domain, SDS-PAGE
36500
theoretical and apparent for hexa-His-tagged C-terminal part (aa168-417), SDS-PAGE
41800
hexa-His-tagged full-length enzyme, SDS-PAGE/Western blot
56800
SDS-PAGE; theoretical for hexa-His-tagged full-length enzyme
72870
theoretical for full-length with N-terminal horseradish peroxide-thioredoxin-tag and C-terminal hexa-His-tag, apparent weight slightly less in SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 29000, His6-tagged catalytic domain, SDS-PAGE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
-
3.5% relative activity at 1 mM
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, stable for at least 1 month
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from Escherichia coli BL21(DE3) Star and TOP10 membrane preparations, nickel affinity chromatography (batch method), in presence of 0.1 mM lauryldimethylamine N-oxide; His-Select nickel affinity gel column chromatography
Ni-NTA column chromatography
-
Ni2+-bound chelating Sepharose column chromatography, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(lambdaDE3) cells
-
expressed in Escherichia coli TOP10 and BL21(DE3) Star cells, and in Salmonella enterica serovar Typhimurium; from genomic DNA, (i) in pET28a for inducible expression of entire coding sequence or C-terminal part with N-terminal hexa-His-tag and subcellular localisation in Escherichia coli BL21(DE3) Star, (ii) in pBAD-DEST49: for inducible expression with N-terminal horseradish peroxide-thioredoxin-tag and C-terminal hexa-His-tag in Escherichia coli TOP10, (iii) in pBluescript II SK(+): for complementation studies with full-length WsaP, C-terminal part (aa168-417), N-terminal part (aa1-314) or a mutant lacking the transmembrane domains (aa311-471) in Escherichia coli strain CWG466 and Salmonella enterica strain MSS2
expressed in Salmonella typhimurium strain MSS2
-
the His6-tagged catalytic domain is expressed in Escherichia coli BL21(DE3) and C43(DE3) cells
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D446A
-
the mutant shows decreased activity compared to the wild type
G393A
-
the mutant shows increased activity compared to the wild type
Show AA Sequence (1530 entries)
Please use the Sequence Search for a specific query.