Part:BBa_K1696002
L-Lactate producing module from Geobacillus stearothermophilus
Enzymes have become important tools in several industries due to their ability to produce chirally pure and complex molecules with interesting biological properties. The NAD(+)-dependent LDH (lactate dehydrogenase, bsLDH) from G. stearothermophilus (formerly Bacillus stearothermophilus) is a particularly crucial enzyme in the pharmaceutical industry and is related to other metabolites in terms of NADH use and regeneration. LDH catalyses the interconversion of pyruvate and lactate using the NADH/NAD(+) pair as a redox cofactor.
References:
[1] N G, Karagüler, R B, Sessions, B, Binay, et al. Protein engineering applications of industrially exploitable enzymes: Geobacillus stearothermophilus LDH and Candida methylica FDH.[J]. Biochem Soc Trans, 2007, 35(Pt 6):1610-1615.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 180
- 1000COMPATIBLE WITH RFC[1000]
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