Information on EC 2.3.2.3 - lysyltransferase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY hide
2.3.2.3
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RECOMMENDED NAME
GeneOntology No.
lysyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-lysyl-tRNALys + phosphatidylglycerol = tRNALys + 3-O-L-lysyl-1-O-phosphatidylglycerol
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacyl group transfer
SYSTEMATIC NAME
IUBMB Comments
L-lysyl-tRNALys:phosphatidylglycerol 3-O-lysyltransferase
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CAS REGISTRY NUMBER
COMMENTARY hide
37257-20-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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a MprF knockout mutant demonstrates a substantial increase in the phosphatidylglycerol:lysylphosphatidylglycerol ratio of the membrane
metabolism
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the C-terminal domain of the enzyme is responsible for the synthesis of lysylphosphatidylglycerol
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
show the reaction diagram
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
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
show the reaction diagram
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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anionic surfactant, e.g. sodium-salt of a fatty acid, and high ionic strength lead to activation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0069
L-lysyl-tRNA
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0.056
phosphatidylglycerol
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000072
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supernatant 10000 x g
0.00000143
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cell crude extract
0.00000326
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membrane fraction
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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steady state assay
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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steady state assay
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
theoretical, MprF(-14) mutant, truncated protein consisting of residues 510-840
48000
theoretical, MprF(-12) mutant, truncated protein consisting of residues 437-840
56000
theoretical, MprF(-10) mutant, truncated protein consisting of residues 363-840
67000
theoretical, MprF(-8) mutant, truncated protein consisting of residues 274-840; theoretical, MprF(-C) mutant, truncated protein consisting of residues 1-586
75000
theoretical, MprF(-6) mutant, truncated protein consisting of residues 219-840
80000
theoretical, MprF(-4) mutant, truncated protein consisting of residues 157-840
88000
theoretical, MprF(-2) mutant, truncated protein consisting of residues 84-840
97000
theoretical, MprF wild-type
100000
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determined by SDS-PAGE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, membrane-bound enzyme extracted with organic solvents, t1/2: 3-5 days
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-20°C, native membrane-bound enzyme, several weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
membrane fractions are prepared by differential centrifugation
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in a Staphylococcus aureus mprF deletion mutant
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expression in Escherichia coli
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for the construction of lysX deletion and complemented derivative Mycobacterium tuberculosis strains
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into the vector pET28
into the vector pET33b for expression in Escherichia coli Rosetta2 DE3, C41 and C43 cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D546A
MprF(-8) mutant, replacement results in slightly reduced production of lysyl-phosphatidylglycerol, same result is obtained when the mutation is introduced into the full-length MprF protein
D731A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
E624A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
E685A
MprF(-8) mutant, replacement results in strongly reduced production of lysyl-phosphatidylglycerol, same result is obtained when the mutation is introduced into the full-length MprF protein
K547A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
K621A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
K806A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
MprF(-10)
mutant, truncated protein consisting of residues 363-840
MprF(-12)
mutant, truncated protein consisting of residues 437-840
MprF(-14)
mutant, truncated protein consisting of residues 510-840
MprF(-2)
mutant, truncated protein consisting of residues 84-840
MprF(-4)
mutant, truncated protein consisting of residues 157-840
MprF(-6)
mutant, truncated protein consisting of residues 219-840
MprF(-8)
mutant, truncated protein consisting of residues 274-840
MprF(-C)
mutant, truncated protein consisting of residues 1-586
R734A
MprF(-8) mutant, exchange leads to complete abrogation of lysyl-phosphatidylglycerol production, same result is obtained when the mutation is introduced into the full-length MprF protein
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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a method to obtain a stable enriched membrane fraction containing MprF, and the techniques necessary to quantitatively monitor its activity in vitro and in vivo is reported
medicine
MprF could be a target for new anti-virulence drugs
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