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. '''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. '''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. | ||
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| - | == Structural highlights == | ||
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Revision as of 07:46, 25 October 2015
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3D Structures of 7,8-diaminopelargonic acid synthetase
Updated on 25-October-2015
References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
