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Enzyme Nomenclature
Information on EC 2.5.1.94 - adenosyl-chloride synthase
Word Map on EC 2.5.1.94
- 2.5.1.94
-
chlorinate
- streptomyces
-
fluorinase
- cattleya
-
polyketide
- tropica
-
salinosporamide
-
anticancer
-
salinispora
- halide
- halogenase
-
non-ribosomal
-
antifungal
- proteasome
-
elaborated
- fluoride
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.5.1.94
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RECOMMENDED NAME
GeneOntology No.
adenosyl-chloride synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + chloride = 5-deoxy-5-chloroadenosine + L-methionine
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:chloride adenosyltransferase
This enzyme, isolated from the marine bacterium Salinispora tropica, catalyses an early step in the pathway leading to biosynthesis of the proteosome inhibitor salinosporamide A. The enzyme is very similar to EC 2.5.1.63, adenosyl-fluoride synthase, but does not accept fluoride.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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a chlorinase knockout mutated strain of Salinispora tropica is able to biosynthesis the fluorinated analogue of salinosporamide A, when the medium was supplemented with 5-deoxy-5’-fluoroadenosine
metabolism
physiological function
metabolism
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the enzyme catalyzes chlorination, the last step in the aspirochlorine pathway, modeling of the aspirochlorine biosynthesis involving an unusual Phe to Gly conversion, overview
metabolism
Salinospora tropica
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the enzyme is responsible for salinosporamide-A biosynthesis
physiological function
SalL functions in an orthogonal manner to biological chlorination reactions to initiate the biosynthesis of a new halogenated polyketide synthase building block
physiological function
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key role of AclH as a chlorinase in the aspirochlorine biosynthesis. Aspirochlorine, or antibiotic A30641, is an epidithiodiketopiperazine toxin distinctive antifungal properties due to selective inhibition of protein biosynthesis produced from Aspergillus oryzae
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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
5-deoxy-5'-chloroadenosine + L-methionine
S-adenosyl-L-methionine + chloride
-
-
-
r
S-adenosyl-L-methionine + bromide
5'-deoxy-5'-bromoadenosine + L-methionine
the enzyme also accepts bromide as substrate (with 90% relative activity compared to chloride) but the brominase activity is probably not biologically relevant in this marine bacterium
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-
r
S-adenosyl-L-methionine + fluoride
5'-deoxy-5'-fluoroadenosine + L-methionine
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-
-
-
r
S-adenosyl-L-methionine + iodide
5'-deoxy-5'-iodoadenosine + L-methionine
the enzyme also accepts iodide as substrate (with 33% relative activity compared to chloride) but the iodinase activity is probably not biologically relevant in this marine bacterium
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-
r
S-adenosyl-L-methionine + chloride
5'-deoxy-5'-chloroadenosine + L-methionine
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-
-
-
?
S-adenosyl-L-methionine + chloride
5'-deoxy-5'-chloroadenosine + L-methionine
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-
-
-
?
S-adenosyl-L-methionine + chloride
5'-deoxy-5'-chloroadenosine + L-methionine
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chlorinase catalyzes chloride ion SN2 substitution at the C5' of S-adenosyl-L-methionine to generate 5'-deoxy-5'-chloroadenosine
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-
?
S-adenosyl-L-methionine + chloride
5'-deoxy-5'-chloroadenosine + L-methionine
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-
-
r
S-adenosyl-L-methionine + chloride
5'-deoxy-5'-chloroadenosine + L-methionine
Salinospora tropica
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-
-
-
r
additional information
?
-
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although this enzyme utilises bromide and even iodide it does not fluorinate
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-
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additional information
?
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the enzyme does not accept fluoride and 5-deoxy-5'-fluoroadenosine as substrates
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-
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additional information
?
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Salinospora tropica
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chlorinase does not accept fluoride ion as a substrate
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-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
S-adenosyl-L-methionine + chloride
5'-deoxy-5'-chloroadenosine + L-methionine
Salinospora tropica
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-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0002
5'-chloro-5'-deoxyadenosine
in 50 mM phosphate buffer (pH 7.9) at 37°C
0.0046
5'-deoxy-5'-iodoadenosine
in 50 mM phosphate buffer (pH 7.9) at 37°C
0.001
S-adenosyl-L-methionine
in 50 mM phosphate buffer (pH 7.9) at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.2
5'-chloro-5'-deoxyadenosine
in 50 mM phosphate buffer (pH 7.9) at 37°C
0.83
5'-deoxy-5'-iodoadenosine
in 50 mM phosphate buffer (pH 7.9) at 37°C
0.2
L-methionine
in 50 mM phosphate buffer (pH 7.9) at 37°C
0.015
S-adenosyl-L-methionine
in 50 mM phosphate buffer (pH 7.9) at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1000
5'-chloro-5'-deoxyadenosine
in 50 mM phosphate buffer (pH 7.9) at 37°C
181.1
5'-deoxy-5'-iodoadenosine
in 50 mM phosphate buffer (pH 7.9) at 37°C
0.0000883
bromide
in 50 mM phosphate buffer (pH 7.9) at 37°C
0.0003
chloride
in 50 mM phosphate buffer (pH 7.9) at 37°C
0.0000192
Iodide
in 50 mM phosphate buffer (pH 7.9) at 37°C
0.077
L-methionine
in 50 mM phosphate buffer (pH 7.9) at 37°C
15
S-adenosyl-L-methionine
in 50 mM phosphate buffer (pH 7.9) at 37°C
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
3 * 30000, in solution as determined by sedimentation velocity studies
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotrimer
homotrimer
3 * 30000, in solution as determined by sedimentation velocity studies
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 28% (w/v) PEG 3350, 0.3 M KCl, 2 mM dithiothreitol, 0.1 M MOPSO, pH 7.0
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene aclH, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis
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gene salL, the gene is located in the middle of this salinosporamide A cluster
Salinospora tropica
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G131S
the mutation leads to the complete loss of all SalL halogenase activities and the inability to crystallize SalL
W129F
the mutant shows 52% chlorinase activity, 76% brominase activity, and 3% iodidase activity compared to the wild type enzyme
Y70T
the mutation results in a two-orders-of-magnitude reduction of SalL activity, the mutant shows 0.07% chlorinase activity, 0.1% brominase activity, and 0.4% iodidase activity compared to the wild type enzyme
Y70T/G131S
the mutant shows 0.3% chlorinase activity, 0.5% brominase activity, and no iodidase activity compared to the wild type enzyme
additional information
additional information
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construction of an aclH deletion mutant of Aspergillus oryzae RIB40 strain, that is inactive with 3-chloro-L-tyrosine and 3-chloro-DL-phenylalanine. The DaclH mutant culture accumulates dechloroaspirochlorine. Complementation by ectopic integration of aclH in the DaclH mutant restores aspirochlorine production
additional information
Salinospora tropica
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gene replacement of gene salL from Salinispora tropica by gene flA, EC 2.5.1.63, encoding fluorinase from Streptomaces cattleya, the recombinant fluorinase is functional in Salinispora tropica
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LINKS TO OTHER DATABASES (specific for EC-Number 2.5.1.94)
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