7,8-diaminopelargonic acid synthase
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<StructureSection load='1qj3' size='350' side='right' caption='Structure of E. coli 7,8-diaminopelargonic acid synthase complex with PLP, KAPA and Na+ ion (purple) (PDB code [[1qj3]]). ' scene='59/595793/Cv/1'> | <StructureSection load='1qj3' size='350' side='right' caption='Structure of E. coli 7,8-diaminopelargonic acid synthase complex with PLP, KAPA and Na+ ion (purple) (PDB code [[1qj3]]). ' scene='59/595793/Cv/1'> | ||
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==Introduction== | ==Introduction== | ||
| - | '''7,8-diaminopelargonic acid synthase''' (also known as BioA synthase or DAPAS ) is an enzyme involved in the biosynthesis of biotin, a vitamin essential for the metabolism of carbohydrates, fats, and proteins. Biotin serves as a cofactor for several carboxylase enzymes involved in important metabolic reactions. | + | '''7,8-diaminopelargonic acid synthase''' (also known as '''BioA synthase''' or '''DAPAS''' ) is an enzyme involved in the biosynthesis of biotin, a vitamin essential for the metabolism of carbohydrates, fats, and proteins. Biotin serves as a cofactor for several carboxylase enzymes involved in important metabolic reactions. |
DAPAS catalyzes a key step in the biotin biosynthesis pathway. It converts pimeloyl-CoA, a seven-carbon Coenzyme A (CoA) thioester, to 7,8-diaminopelargonic acid (DAPA), which is a precursor molecule for biotin synthesis. | DAPAS catalyzes a key step in the biotin biosynthesis pathway. It converts pimeloyl-CoA, a seven-carbon Coenzyme A (CoA) thioester, to 7,8-diaminopelargonic acid (DAPA), which is a precursor molecule for biotin synthesis. | ||
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== Function == | == Function == | ||
| - | '''DAPAS''' catalyzes the amino transfer from S-adenosylmethionine to 7-keto-8-pelargonic acid (KAPA) to produce S-adenosyl-4-methylthio-2-oxobutanoate and 7,8-diaminopelargonic acid. DAPAS is a pyridoxal phosphate (PLP)-dependent enzyme.<ref>PMID:12379100</ref> '''Bifunctional DAPAS/dethiobiotin synthase''' ( | + | '''DAPAS''' catalyzes the amino transfer from S-adenosylmethionine to 7-keto-8-pelargonic acid (KAPA) to produce S-adenosyl-4-methylthio-2-oxobutanoate and 7,8-diaminopelargonic acid. DAPAS is a pyridoxal phosphate (PLP)-dependent enzyme.<ref>PMID:12379100</ref> '''Bifunctional DAPAS/dethiobiotin synthase''' ('''DAPAS/DTBS''') catalyzes the above reaction and the conversion of 7,8-diaminonanoate, ATP and CO2 to ADP, phosphate and dethiobiotin. |
*<scene name='59/595793/Cv/7'>KAPA binding site</scene>. Water molecules are shpwn as red spheres. | *<scene name='59/595793/Cv/7'>KAPA binding site</scene>. Water molecules are shpwn as red spheres. | ||
*<scene name='59/595793/Cv/8'>PLP binding site</scene> (residues of chain B are in yellow and labeled (B). | *<scene name='59/595793/Cv/8'>PLP binding site</scene> (residues of chain B are in yellow and labeled (B). | ||
Current revision
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References
- ↑ Eliot AC, Sandmark J, Schneider G, Kirsch JF. The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation. Biochemistry. 2002 Oct 22;41(42):12582-9. PMID:12379100
- ↑ Kack H, Sandmark J, Gibson K, Schneider G, Lindqvist Y. Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes. J Mol Biol. 1999 Aug 27;291(4):857-76. PMID:10452893 doi:http://dx.doi.org/10.1006/jmbi.1999.2997
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