7,8-diaminopelargonic acid synthase

Introduction

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.

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.

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.

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.

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.

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

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.^[1] 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.

• . Water molecules are shpwn as red spheres.
• (residues of chain B are in yellow and labeled (B).
• (PDB code 1qj3).^[2]
• .

3D Structures of 7,8-diaminopelargonic acid synthase

7,8-diaminopelargonic acid synthase 3D structures