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Naphthoate synthase

Class of enzymes

Naphthoate synthase

Class of enzymes

FieldValue
Name1,4-dihydroxy-2-naphthoyl-CoA synthase
EC_number4.1.3.36
CAS_number72506-71-9
GO_code0008935
image4qii.jpg
width270
caption1,4-Dihydroxy-2-naphthoyl-CoA synthase hexamer, Mycobacterium tuberculosis

Nomenclature

MenB is part of the crotonase fold super family, named after the crotonase fold in their structure. The systematic name for MenB is 4-(2-carboxyphenyl)-4-oxobutanoyl-CoA dehydratase (cyclizing). Other common names include:

  • Naphthoate synthase
  • 1,4-dihydroxy-2-naphthoate synthase
  • Dihydroxynaphthoate synthase
  • DHNA-CoA synthase

Reaction

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It was originally thought that the product of this reaction had an oxygen where the SCoA currently resides, however; new research has shown that MenB only catalyzes the above reaction. There is a different enzyme that cleaves the SCoA and attaches the oxygen.

Structure

The channel formed by alpha helices that can be seen in the middle of the enzyme leads to the active site. This opening exists on both top and bottom of the enzyme, allowing substrates different entry points to the active site, which rests in the middle of the enzyme.

Six different crystal structures have been studied for MenB in Escherichia coli their PDB codes are: 3t88, 3t89, 4els, 4elw, 4elx, and 4i42.

Other structures have been solved for this class of enzymes, with PDB accession codes , , , , and .

Homologs

Homologous genes MenB exist in many different organisms, such as; Galium mollugo, Geobacillus kaustophilus, Mycobacterium phlei, Mycobacterium tuberculosis, Spinacia oleracea, and Staphylococcus aureus.

MenB is only found in biosynthesis pathways in plants and bacteria, it does not exist in any other organisms. However, mammals require vitamin K in their diet because it is vital in the blood clotting process.

Cofactors/Inhibitors

MenB does not require any cofactors to catalyze the reaction.

In the organism Escherichia coli three inhibitors exist: 1-hydroxy-2-naphthoyl-CoA, 2,3-dihydroxybenzoyl-CoA, and 2,4-dihydroxybenzoyl-CoA.

References

References

  1. (April 26, 2013). "Structural Basis of the Induced-Fit Mechanism of 1,4-Dihydroxy-2-Naphthoyl Coenzyme A Synthase from the Crotonase Fold Superfamily". PLOS ONE.
  2. (July 2014). "Information on EC 4.1.3.36 - 1,4-dihydroxy-2-naphthoyl-CoA synthase".
  3. (2011). "Phylloquinone (Vitamin K1): function, enzymes and genes". Academic Press.
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