7,8-diaminopelargonic acid synthase
From Proteopedia
(Difference between revisions)
m (7,8-diaminopelargonic acid synthetase moved to 7,8-diaminopelargonic acid synthase: requested by Editor) |
|||
| Line 4: | Line 4: | ||
'''7,8-diaminopelargonic acid synthase''' (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 synthase''' (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 synthase''' (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 synthase''' (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/7'>KAPA binding site</scene>. | + | *<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). | ||
*<scene name='59/595793/Cv/9'>KAPA/PLP binding sites together</scene> (PDB code [[1qj3]]).<ref>PMID:10452893</ref> | *<scene name='59/595793/Cv/9'>KAPA/PLP binding sites together</scene> (PDB code [[1qj3]]).<ref>PMID:10452893</ref> | ||
Revision as of 13:56, 28 October 2019
| |||||||||||
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
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
