7,8-diaminopelargonic acid synthase
From Proteopedia
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'''7,8-diaminopelargonic acid synthetase''' (DAPAS) is part of the biotin biosynthesis pathway. 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 synthetase''' (DAPS/DTBS) catalyzes the above reaction and the conversion of 7,8-diaminonanoate, ATP and CO2 to ADP, phosphate and dethiobiotin. | '''7,8-diaminopelargonic acid synthetase''' (DAPAS) is part of the biotin biosynthesis pathway. 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 synthetase''' (DAPS/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/ | + | *<scene name='59/595793/Cv/7'>KAPA binding site</scene>. |
| - | *<scene name='59/595793/Cv/ | + | *<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/ | + | *<scene name='59/595793/Cv/9'>KAPA/PLP binding sites together</scene> (PDB code [[1qj3]]).<ref>PMID:10452893</ref> |
</StructureSection> | </StructureSection> | ||
Revision as of 11:54, 17 December 2018
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3D Structures of 7,8-diaminopelargonic acid synthetase
Updated on 17-December-2018
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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