Information on EC 2.3.2.3 - lysyltransferase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
2.3.2.3
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RECOMMENDED NAME
GeneOntology No.
lysyltransferase
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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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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aminoacyl group transfer
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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
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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
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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
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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
L-lysyl-tRNALys + phosphatidylglycerol
tRNALys + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol
show the reaction diagram
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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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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steady state assay
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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steady state assay
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
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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
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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
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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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Show AA Sequence (3917 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.3.2.3)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)