7,8-diaminopelargonic acid synthase

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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.
'''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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The enzyme 7,8-diaminopelargonic acid synthase 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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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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The reaction catalyzed by 7,8-diaminopelargonic acid synthase 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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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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Deficiencies or disruptions in the activity of 7,8-diaminopelargonic acid synthase 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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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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Understanding the structure and function of 7,8-diaminopelargonic acid synthase 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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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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In summary, 7,8-diaminopelargonic acid synthase (BioA or DAPA synthase) 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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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.
== Function ==
== Function ==

Revision as of 08:58, 15 June 2023

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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