Pantothenate (or pantothenic acid) is a B vitamin used as a precursor for coenzyme A (CoA), which is a cofactor needed in metabolism (for instance, acetyl-CoA). The biosynthesis is pretty straightforward. taking either dihydroxyisovalerate or valine to ketoisovalerate, which is then converted into ketopantoate (using a folate cofactor) and then reduced to pantoate. Afterwards, a decarboxylated aspartate, called beta alanine, is condensed with the pantoate to generate pantothenate.
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References and Resources
Biosynthesis of Pantothenic Acid and Coenzyme A
Organisation of the pantothenate (vitamin B5) biosynthesis pathway in higher plants
Function and maturation of the Fe–S center in dihydroxy acid dehydratase from Arabidopsis
The active site of the Mycobacterium tuberculosis branched-chain amino acid biosynthesis enzyme dihydroxyacid dehydratase contains a 2Fe–2S cluster
The Role and Properties of the Iron-Sulfur Cluster in Escherichia coli Dihydroxy-acid Dehydratase
The substrate specificity, enantioselectivity and structure of the (R)-selective amine: pyruvate transaminase from Nectria haematococca
Structure ofE. Coli Ketopantoate Hydroxymethyl Transferase Complexed with Ketopantoate and Mg2+,Solved by Locating 160 Selenomethionine Sites
Experimental and Metabolic Modeling Evidence for a Folate-Cleaving Side-Activity of Ketopantoate Hydroxymethyltransferase (PanB)
Pantothenate biosynthesis in higher plants: advances and challenges
Crystal Structure of Escherichia coli Ketopantoate Reductase in a Ternary Complex with NADP+ and Pantoate Bound
Studies towards the selective inhibition of β-alanine pathways in Mycobacterium tuberculosis
An activator for pyruvoyl-dependent l-aspartate α-decarboxylase is conserved in a small group of the γ-proteobacteria including Escherichia coli
The Structure of the PanD/PanZ Protein Complex Reveals Negative Feedback Regulation of Pantothenate Biosynthesis by Coenzyme A
The Mechanism of Regulation of Pantothenate Biosynthesis by the PanD−PanZ·AcCoA Complex Reveals an Additional Mode of Action for the Antimetabolite N‑Pentyl Pantothenamide (N5-Pan)
Novel cofactors via post-translational modifications of enzyme active sites
Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate
A Fragment-Based Approach to Probing Adenosine Recognition Sites by Using Dynamic Combinatorial Chemistry
Characterization and validation of Entamoeba histolytica pantothenate kinase as a novel anti-amebic drug target
PDB Codes
6OVT – IlvD Dihydroxy acid Dehydratase (DHAD) from Mycobacterium tuberculosis
1M3U – PanB Ketopentoate Hydroxymethyltransferase
2OFP – PanE Ketopentoate Reductase
4CRZ – Aspartate 1 Decarboxylase
4CS0 – Aspartate 1 Decarboxylase
51S7 – Aspartate 1 Decarboxylase
1UHD – Aspartate 1 Decarboxylase
1N2O – PanC Pantothenate Synthetase
3Q12 – PanC Pantothenate Synthetase
2A7X – PanC Pantothenate Synthetase
1N2G – PanC Pantothenate Synthetase
1N2I – PanC Pantothenate Synthetase
