Information on EC 2.5.1.28 - dimethylallylcistransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.5.1.28
-
RECOMMENDED NAME
GeneOntology No.
dimethylallylcistransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
alkenyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
trichome monoterpenes biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
dimethylallyl-diphosphate:isopentenyl-diphosphate dimethylallylcistransferase
This enzyme will not use larger prenyl diphosphates as efficient donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-79-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
monoterpene-producing accession LA2409, gene NDPS1 of the CPT1 locus
UniProt
Manually annotated by BRENDA team
gene SlCPT1
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
homology modeling and three-dimensional structure
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dimethylallyl diphosphate + isopentenyl diphosphate
diphosphate + neryl diphosphate
show the reaction diagram
neryl diphosphate + isopentenyl diphosphate
diphosphate + (2Z,6Z)-farnesyl diphosphate
show the reaction diagram
mutant NDPS1-M10
-
-
?
additional information
?
-
the relative positioning of aromatic amino acid residues at positions 100 and 107 determines the ability of these enzymes to synthesize neryl diphosphate or (2Z,6Z)-farnesyl diphosphate
-
-
-
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
dimethylallyl diphosphate + isopentenyl diphosphate
diphosphate + neryl diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.047 - 0.177
dimethylallyl diphosphate
0.111 - 0.157
isopentenyl diphosphate
0.014 - 0.097
neryl diphosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0064 - 0.2
dimethylallyl diphosphate
0.011 - 0.16
isopentenyl diphosphate
0.18 - 3.7
neryl diphosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15 - 1.6
dimethylallyl diphosphate
157
0.33 - 1.8
isopentenyl diphosphate
113
0.28 - 1.8
neryl diphosphate
1451
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
type VI glandular trichome
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene NDPS1 of the CPT1 locus, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, functional expression of codon-optimized synthetic version of CPT1 of accession LA2409, a monoterpene-producing accession, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli
gene SlCPT1, located on chromosome 8, and other gene of the CPT gene family, DNA and amino acid sequence determination and analysis, phylogenetic analysis
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E98D/Y100S/I106L/I107F
site-directed mutagenesis, mutant M4
E98D/Y100S/I107F
site-directed mutagenesis, mutant M3V2
Y100S/I106L/I107F
site-directed mutagenesis, mutant M3V1
Y100S/I107F
site-directed mutagenesis, mutant M2
additional information