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Review
. 2008 Apr;12(2):118-25.
doi: 10.1016/j.cbpa.2008.02.006. Epub 2008 Apr 2.

Cofactor biosynthesis--still yielding fascinating new biological chemistry

Tadhg P Begley  1 , Abhishek Chatterjee, Jeremiah W Hanes, Amrita Hazra, Steven E Ealick
Affiliations
Review

Cofactor biosynthesis--still yielding fascinating new biological chemistry

Tadhg P Begley et al. Curr Opin Chem Biol. 2008 Apr.

Abstract

This mini review covers recent advances in the mechanistic enzymology of cofactor biosynthesis.

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Figures

Figure 1
Figure 1
Thiamin phosphate 3 is biosynthesized by coupling the thiazole 1 with the pyrimidine 2.
Figure 2
Figure 2
Mechanistic proposal for the formation of the thiamin thiazole 1 in bacteria. ThiS represents the sulfide carrier protein.
Figure 3
Figure 3
Mechanistic proposal for the ThiH-catalyzed formation of glycine imine (14) under anaerobic conditions.
Figure 4
Figure 4
Labeling studies that map out the complex conversion of aminoimidazole ribotide to the thiamin pyrimidine.
Figure 5
Figure 5
Mechanistic proposal for the formation of the thiamin thiazole (41) in S. cerevisiae.
Figure 6
Figure 6
The pyrimidine moiety of thiamin in S. cerevisiae is formed by a remarkable reaction sequence in which the histidine atoms labeled in blue and the PLP atoms labeled in red are incorporated into the pyrimidine 44.
Figure 7
Figure 7
A new thiamin salvage pathway for the recycling of the pyrimidine of thiazole-degraded thiamin.
Figure 8
Figure 8
MoaA and MoaC catalyze the formation of Precursor Z (49) on the molybdopterin biosynthetic pathway.
Figure 9
Figure 9
A mechanistic proposal for the formation of PLP (43). Pdx1 represents the pyridoxal phosphate synthase.
Figure 10
Figure 10
Shown is the major bacterial pathway for the formation of the quinolinic acid (68) precursor to NAD 28.
Figure 11
Figure 11
Shown is the mechanistic proposal for the formation of quinolinic acid 68 from hydroxyanthranilate (69).
Figure 12
Figure 12
Mechanistic proposal for the oxidative decarboxylation of coproporphyrinogen III (74) to protoporphyrinogen IX (75).
Figure 13
Figure 13
Mechanistic proposal for the oxidation of FMN 79 to dimethylbenzimidazole 87.
See this image and copyright information in PMC

References

    1. Hanes JW, Ealick SE, Begley TP. Thiamin Phosphate Synthase: The Rate of Pyrimidine Carbocation Formation. Journal of the American Chemical Society. 2007;129:4860–4861. Structural and kinetic characterization of the pyrimidine carbocation intermediate generated at the active site of thiamin phosphate synthase

    1. Chatterjee A, Han X, McLafferty FW, Begley TP. Biosynthesis of thiamin thiazole: determination of the regiochemistry of the S/O acyl shift by using 1,4-dideoxy-D-xylulose-5-phosphate. Angewandte Chemie, International Edition. 2006;45:3507–3510. Determination that the acyl shift in thiamin thiazole biosynthesis occurs to the C3 hydroxyl of DXP

    1. Dorrestein PC, Zhai H, McLafferty FW, Begley TP. The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur transfer mediated by the sulfur carrier protein ThiS. Chemistry & Biology. 2004;11:1373–1381. Mechanistic characterization of the bacterial thiazole synthase

    1. Dorrestein PC, Zhai H, Taylor SV, McLafferty FW, Begley TP. The biosynthesis of the thiazole phosphate moiety of thiamin (vitamin B1): the early steps catalyzed by thiazole synthase. Journal of the American Chemical Society. 2004;126:3091–3096. Mechanistic characterization of the early steps in bacterial thiazole biosynthesis.

    1. Duda DM, Walden H, Sfondouris J, Schulman BA. Structural analysis of Escherichia coli ThiF. Journal of Molecular Biology. 2005;349:774–786. The structure of the enzyme involved in the activation of the sulfur carrier protein involved in thiazole biosynthesis

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