Function
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.
Disease
Relevance
Structural highlights
3D Structures of 7,8-diaminopelargonic acid synthetase
Updated on 24-August-2014
7,8-diaminopelargonic acid synthetase
1dty, 1qj5 – EcDAPAS + PLP - Escherichia coli
1mgv, 1s07 – EcDAPAS (mutant) + PLP
3bv0 – MtDAPAS (mutant) + PLP – Mycobacterium tuberculosis
3dod – BsDAPAS + PLP – Bacillus subtilis
3drd – BsDAPAS + PLP
1s06, 1s08, 1s09, 1s0a – EcDAPAS (mutant) + PLP derivative
4a0g – AtDAPAS + PLP – Arabidopsis thaliana
4a0f – AtDAPAS (mutant) + PLP
7,8-diaminopelargonic acid synthetase complex
1qj3 – EcDAPAS + PLP + KAPA
1mly, 1mlz – EcDAPAS + PLP + amiclenomycin
3du4 – BsDAPAS + PLP + KAPA
4a0h – AtDAPAS + PLP + KAPA
4cxq – MtDAPAS + PLP + KAPA
3lv2 – MtDAPAS + PLP + sinefungin
3tft, 3tfu – MtDAPAS + PLP + inhibitor
4mqp, 4mqq, 4mqr – MtDAPAS + inhibitor
Bifunctional 7,8-diaminopelargonic acid synthetase/dethiobiotin synthetase
4a0f, 4a0g – AtDAPAS + PLP
4a0r – AtDAPAS + PLP + dethiobiotin
4a0h – AtDAPAS + PLP + keto-aminopelargonic acid
References
