Part:BBa_K4689070
Alcohol dehydrogenase (adhA)
ADHA Alcohol dehydrogenase A, often referred to as AdhA, is a key enzyme involved in the isobutanol pathway, which is a metabolic route responsible for the biosynthesis of isobutanol. AdhA belongs to the class of enzymes known as alcohol dehydrogenases, which play a central role in the conversion of alcohols to their corresponding aldehydes or ketones by catalyzing the transfer of electrons and protons.
Significance in the Isobutanol Pathway:
AdhA's significance in the isobutanol pathway lies in its ability to catalyze a crucial step in the final stages of isobutanol synthesis. Specifically, AdhA is responsible for converting the aldehyde 2-ketoisobutyraldehyde (2-KIBA) into isobutanol. This chemical transformation is essential because it represents the final and key step in the conversion of intermediates into the desired end product, isobutanol. The conversion of 2-KIBA to isobutanol by AdhA involves the reduction of the aldehyde group to an alcohol group. This reaction not only yields isobutanol, a valuable biofuel and chemical precursor, but it also regenerates the cofactors (such as NADH) used in the preceding reactions of the isobutanol pathway. This regeneration of cofactors is critical for sustaining the pathway's enzymatic reactions, allowing for a continuous production of isobutanol.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 442
- 1000COMPATIBLE WITH RFC[1000]
REFERENCES
1.Smith, K. M., Cho, K. M., & Liao, J. C. (2010). Engineering Corynebacterium glutamicum for isobutanol production. Applied microbiology and biotechnology, 87, 1045-1055.
2.Atsumi, S., Wu, T. Y., Eckl, E. M., Hawkins, S. D., Buelter, T., & Liao, J. C. (2010). Engineering the isobutanol biosynthetic pathway in Escherichia coli by comparison of three aldehyde reductase/alcohol dehydrogenase genes. Applied microbiology and biotechnology, 85, 651-657.
None |