7,8-diaminopelargonic acid synthase

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<StructureSection load='1qj3' size='350' side='right' caption='Structure of E. coli 7,8-diaminopelargonic acid synthetase complex with PLP, KAPA and Na+ ion (purple) (PDB code [[1qj3]]). ' scene='59/595793/Cv/1'>
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<StructureSection load='1qj3' size='350' side='right' caption='Structure of E. coli 7,8-diaminopelargonic acid synthase complex with PLP, KAPA and Na+ ion (purple) (PDB code [[1qj3]]). ' scene='59/595793/Cv/1'>
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__TOC__
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==Introduction==
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'''7,8-diaminopelargonic acid synthase''' (also known as '''BioA synthase''' or '''DAPAS''' ) is an enzyme involved in the biosynthesis of biotin, a vitamin essential for the metabolism of carbohydrates, fats, and proteins. Biotin serves as a cofactor for several carboxylase enzymes involved in important metabolic reactions.
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== Function ==
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DAPAS catalyzes a key step in the biotin biosynthesis pathway. It converts pimeloyl-CoA, a seven-carbon Coenzyme A (CoA) thioester, to 7,8-diaminopelargonic acid (DAPA), which is a precursor molecule for biotin synthesis.
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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.
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The reaction catalyzed by DAPAS involves the decarboxylation of pimeloyl-CoA and the subsequent addition of an amino group to the resulting intermediate, forming DAPA. This enzymatic step is crucial in the conversion of the precursor molecule into the biotin ring structure.
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*<scene name='59/595793/Cv/2'>KAPA binding site</scene>.
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*<scene name='59/595793/Cv/5'>PLP binding site</scene> (residues of chain B are in yellow and labeled (B).
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*<scene name='59/595793/Cv/6'>KAPA/PLP binding sites together</scene> (PDB code [[1qj3]]).<ref>PMID:10452893</ref>
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</StructureSection>
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== 3D Structures of 7,8-diaminopelargonic acid synthetase==
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Deficiencies or disruptions in the activity of DAPAS can lead to a biotin biosynthesis disorder known as biotin auxotrophy. In such cases, individuals are unable to produce sufficient biotin, requiring exogenous supplementation to meet their biotin requirements.
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*7,8-diaminopelargonic acid synthetase
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Understanding the structure and function of DAPAS has contributed to our knowledge of biotin biosynthesis and the importance of this vitamin in various biological processes. Additionally, the enzyme has been a target for the development of antimicrobial agents, as inhibiting the biotin biosynthesis pathway can be a strategy to disrupt the growth of certain pathogens.
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**[[1dty]], [[1qj5]] – EcDAPAS + PLP - ''Escherichia coli'' <br />
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In summary, DAPAS is an enzyme involved in the biosynthesis of biotin. It catalyzes the conversion of pimeloyl-CoA to 7,8-diaminopelargonic acid (DAPA), a precursor molecule for biotin synthesis. This enzyme plays a critical role in biotin biosynthesis and is important for various metabolic processes that rely on biotin as a cofactor.
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**[[1mgv]], [[1s07]] – EcDAPAS (mutant) + PLP <br />
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**[[3bv0]] – MtDAPAS (mutant) + PLP – ''Mycobacterium tuberculosis''<br />
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**[[3dod]] – BsDAPAS + PLP – ''Bacillus subtilis''<br />
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**[[3drd]] – BsDAPAS + PLP <br />
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**[[1s06]], [[1s08]], [[1s09]], [[1s0a]] – EcDAPAS (mutant) + PLP derivative<br />
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**[[4a0g]] – AtDAPAS + PLP – ''Arabidopsis thaliana''<br />
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**[[4a0f]] – AtDAPAS (mutant) + PLP <br />
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*7,8-diaminopelargonic acid synthetase complex
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== Function ==
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'''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''' ('''DAPAS/DTBS''') catalyzes the above reaction and the conversion of 7,8-diaminonanoate, ATP and CO2 to ADP, phosphate and dethiobiotin.
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*<scene name='59/595793/Cv/7'>KAPA binding site</scene>. Water molecules are shpwn as red spheres.
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*<scene name='59/595793/Cv/8'>PLP binding site</scene> (residues of chain B are in yellow and labeled (B).
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*<scene name='59/595793/Cv/9'>KAPA/PLP binding sites together</scene> (PDB code [[1qj3]]).<ref>PMID:10452893</ref>
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*<scene name='59/595793/Cv/10'>Na coordination site</scene>.
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**[[1qj3]] – EcDAPAS + PLP + KAPA<br />
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== 3D Structures of 7,8-diaminopelargonic acid synthase==
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**[[1mly]], [[1mlz]] – EcDAPAS + PLP + amiclenomycin<br />
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[[7,8-diaminopelargonic acid synthase 3D structures]]
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**[[3du4]] – BsDAPAS + PLP + KAPA<br />
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**[[4a0h]] – AtDAPAS + PLP + KAPA<br />
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**[[4cxq]] – MtDAPAS + PLP + KAPA<br />
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**[[3lv2]] – MtDAPAS + PLP + sinefungin<br />
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**[[3tft]], [[3tfu]] – MtDAPAS + PLP + inhibitor<br />
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**[[4mqp]], [[4mqq]], [[4mqr]] – MtDAPAS + inhibitor<br />
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*Bifunctional 7,8-diaminopelargonic acid synthetase/dethiobiotin synthetase
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</StructureSection>
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**[[4a0f]], [[4a0g]] – AtDAPAS + PLP <br />
 
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**[[4a0r]] – AtDAPAS + PLP + dethiobiotin<br />
 
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**[[4a0h]] – AtDAPAS + PLP + keto-aminopelargonic acid<br />
 
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}}
 
== References ==
== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Structure of E. coli 7,8-diaminopelargonic acid synthase complex with PLP, KAPA and Na+ ion (purple) (PDB code 1qj3).

Drag the structure with the mouse to rotate

References

  1. ↑ 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
  2. ↑ 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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