Information on EC 3.1.2.28 - 1,4-dihydroxy-2-naphthoyl-CoA hydrolase

for references in articles please use BRENDA:EC3.1.2.28
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.1.2.28
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RECOMMENDED NAME
GeneOntology No.
1,4-dihydroxy-2-naphthoyl-CoA hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of thioester
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1,4-dihydroxy-2-naphthoate biosynthesis
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Ubiquinone and other terpenoid-quinone biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
1,4-dihydroxy-2-naphthoyl-CoA hydrolase
This enzyme participates in the synthesis of menaquinones [4], phylloquinone [3], as well as several plant pigments [1,2]. The enzyme from the cyanobacterium Synechocystis sp. PCC 6803 does not accept benzoyl-CoA or phenylacetyl-CoA as substrates [3].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
knockout mutant accumulates 1,4-dihydroxy-2-naphthoyl-CoA, contains 13fold less phylloquinone than the wild-type and displays typical photosensitivity to high light intensities associated with phylloquinone deficiency in cyanobacteria
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
1,4-dihydroxy-2-naphthoyl-CoA + H2O
CoA + 1,4-dihydroxy-2-naphthoate
show the reaction diagram
1-hydroxy-2-naphthoyl-CoA + H2O
CoA + 1-hydroxy-2-naphthoate
show the reaction diagram
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-
-
?
3,4-dihydroxybenzoyl-CoA + H2O
CoA + 3,4-dihydroxybenzoate
show the reaction diagram
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-
-
?
3,5-dihydroxybenzoyl-CoA + H2O
CoA + 3,5-dihydroxybenzoate
show the reaction diagram
-
-
-
?
salicylyl-CoA + H2O
CoA + salicylate
show the reaction diagram
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-
-
?
additional information
?
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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
1,4-dihydroxy-2-naphthoyl-CoA + H2O
CoA + 1,4-dihydroxy-2-naphthoate
show the reaction diagram
Q55777
the reaction is involved in phylloquinone (vitamin K1) biosynthesis
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0025 - 0.033
1,4-dihydroxy-2-naphthoyl-CoA
0.008
1-hydroxy-2-naphthoyl-CoA
pH 7.0, 25°C
0.0269
3,4-dihydroxybenzoyl-CoA
pH 7.0, 25°C
0.0265
3,5-dihydroxybenzoyl-CoA
pH 7.0, 25°C
0.073
salicylyl-CoA
pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.13 - 6.2
1,4-dihydroxy-2-naphthoyl-CoA
14.8
1-hydroxy-2-naphthoyl-CoA
pH 7.0, 25°C
23.2
3,4-dihydroxybenzoyl-CoA
pH 7.0, 25°C
12.6
3,5-dihydroxybenzoyl-CoA
pH 7.0, 25°C
93
salicylyl-CoA
pH 7.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
400 - 2500
1,4-dihydroxy-2-naphthoyl-CoA
1900
1-hydroxy-2-naphthoyl-CoA
pH 7.0, 25°C
860
3,4-dihydroxybenzoyl-CoA
pH 7.0, 25°C
480
3,5-dihydroxybenzoyl-CoA
pH 7.0, 25°C
1300
salicylyl-CoA
pH 7.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.23
pH 7.0, 30°C, incubation in the dark
1.97
pH 7.0, 30°C, incubation in the dark
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Synechocystis sp. (strain PCC 6803 / Kazusa)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15478
x * 15478, calculated from sequence
15700
4 * 15700, calculated
17000
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4 * 17000, calculated
62500
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sedimentation-equilibrium ultracentrifugation
77400
sedimentation-equilibrium ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 15478, calculated from sequence
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.9 A resolution. The core structure is defined by a 5-6-stranded antiparallel beta-sheet that partially wraps around a prominent five-turn alpha-helix. Isoform DHNAT1 has a 27-amino-acid extension at its N-terminus. DHNAT1 is a facial tetramer that features a dimer-dimer interface near the hotdog alpha-helices, which point inward towards the center of the tetramer. The binding site for substrate 1,4-dihydroxy-2-naphthoyl-CoA spans the dimer interface
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to 1.9 A resolution. The core structure is defined by a 5-6-stranded antiparallel beta-sheet that partially wraps around a prominent five-turn alpha-helix. Isoform Slr0204 has a 25-amino-acid extension at its C-terminus, residues 113-138. Slr0204 is a facial tetramer that features a dimer-dimer interface near the hotdog alpha-helices, which point inward towards the center of the tetramer. The binding site for substrate 1,4-dihydroxy-2-naphthoyl-CoA spans the dimer interface
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as a recombinant His-fusion protein
expression in Escherichia coli
expression in Escherichia coli; expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E57Q
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active site mutant, modeling of substrate bound to active site
D16N
active site mutant, modeling of substrate bound to active site
Show AA Sequence (1082 entries)
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