4.1.3.36: 1,4-dihydroxy-2-naphthoyl-CoA synthase
This is an abbreviated version!
For detailed information about 1,4-dihydroxy-2-naphthoyl-CoA synthase, go to the full flat file.
Word Map on EC 4.1.3.36
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4.1.3.36
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menaquinone
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tuberculosis
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crotonase
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1,4-dihydroxy-2-naphthoic
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hexamer
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o-succinylbenzoyl-coa
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o-succinylbenzoic
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oxyanion
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induced-fit
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claisen
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reorientation
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tetrahedral
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osb-coa
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phlei
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5'-triphosphate
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trimer-trimer
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enzyme-ligand
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medicine
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drug development
- 4.1.3.36
- menaquinone
- tuberculosis
- crotonase
-
1,4-dihydroxy-2-naphthoic
-
hexamer
- o-succinylbenzoyl-coa
-
o-succinylbenzoic
-
oxyanion
-
induced-fit
-
claisen
-
reorientation
-
tetrahedral
-
osb-coa
- phlei
- 5'-triphosphate
-
trimer-trimer
-
enzyme-ligand
- medicine
- drug development
Reaction
Synonyms
1,4-dihydroxy-2-naphthoate synthetase, 1,4-dihydroxy-2-naphthoyl coenzyme A synthase, 1,4-dihydroxy-2-naphthoyl-CoA synthase, 1,4-dihydroxy-2-naphthoyl-coenzyme synthase, DHNA synthetase, DHNA-CoA synthase, dihydroxynaphthoate synthase, Dihydroxynaphthoic acid synthetase, MenB, naphthoate synthase, naphthoate synthase (MenB), Rv0548c, synthase, 1,4-dihydroxy-2-naphthoate
ECTree
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General Information
General Information on EC 4.1.3.36 - 1,4-dihydroxy-2-naphthoyl-CoA synthase
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metabolism
physiological function
additional information
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the enzyme catalyzes a carbon-carbon bond formation reaction in the biosynthesis of both vitamin K1 and K2
metabolism
the enzyme catalyzes a carbon-carbon bond formation reaction in the biosynthesis of both vitamin K1 and K2
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the enzyme is an essential enzyme in vitamin K biosynthesis
physiological function
the enzyme is an essential enzyme in vitamin K biosynthesis
active site structure, catalytically essential is Asp185 in the active site, residues Gly77 and Gly123 form an oxyanion hole for stabilization of the enolate intermediate, a hydrophobic patch consisting of Leu96, Val98, and Leu99 for recognition and interaction with the nonpolar aromatic ring of the substrate, and other catalytically essential motifs consisting of Ser151, Asp153, and Tyr248 from a different subunit, detailed overview and modeling
additional information
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active site structure, catalytically essential is Gly156 in the active site, residues Gly86 and Gly133 form an oxyanion hole for stabilization of the enolate intermediate, a hydrophobic patch consisting of Leu106, Val108, and Leu109 for recognition and interaction with the nonpolar aromatic ring of the substrate, and other catalytically essential motifs consisting of Ser161, Asp163, and Tyr258 from a different subunit, detailed overview and modeling
additional information
enzyme structure in complex with a product analogue, the structural changes include the folding of an active-site loop into a beta-hairpin and significant reorientation of a helix at the carboxy terminus. A new interface is formed between the ordered loop and the reoriented helix, both of which also form additional interactions with the coenzyme A moiety of the ligand
additional information
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enzyme structure in complex with a product analogue, the structural changes include the folding of an active-site loop into a beta-hairpin and significant reorientation of a helix at the carboxy terminus. A new interface is formed between the ordered loop and the reoriented helix, both of which also form additional interactions with the coenzyme A moiety of the ligand