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/2'>KAPA binding site</scene>. | |
</StructureSection> | </StructureSection> | ||
Revision as of 09:42, 6 January 2016
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3D Structures of 7,8-diaminopelargonic acid synthetase
Updated on 06-January-2016
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
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