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![[Figure 1]](rr5052fig1mag.jpg)
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Figure 1
(a) Biosynthetic pathway to pantothenate in bacteria. β-Alanine is synthesized via the decarboxylation of L-aspartate by aspartate decarboxylase (ADC). Pantothenate synthetase (PS) catalyses the ATP-dependent ligation of β-alanine with D-pantoate to form pantothenate. Pantoate is formed from α-ketoisovalerate via hydroxymethylation by ketopantoate hydroxymethyltransferase (KPHMT) and reduction by ketopantoate reductase (KPR). (b) Pathway for the formation of the pyruvoyl-dependent cofactor in ADC and other pyruvoyl-dependent enzymes from the zymogenic form (termed the π-chain). The β-hydroxyl of Ser25 attacks the carbonyl of the previous amino-acid residue (i) to form an oxyoxazolidine intermediate, which decomposes (ii) to form an ester intermediate. E1cB elimination (iii) forms a N-terminal dehydroalanyl residue which is hydrolysed (iv) to form the pyruvoyl cofactor (the α-chain). The ester intermediate can also be hydrolysed to yield the inactive α′-chain (v). (c) Schematic of the ADC active site based on the structure of the WT zymogen reported by Schmitzberger et al. (2003  ). The β-hydroxyl group forms a hydrogen bond to the side-chain amide of Asn72, and the backbone carbonyl of Gly24 forms a hydrogen bond to the β-hydroxyl of Thr57. The phenolic hydroxyls of both Tyr58 and Tyr22 (not shown) are candidates to act as a base to deprotonate the hydroxyl of Ser25. |
![[Figure 1]](rr5052fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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