Part:BBa_K4588022:Design

D-Lactate dehydrogenase (''E. coli''), DLDH

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE WITH RFC[1000]

Biology

The organism this gene is initially expressed in is Escherichia coli.

E. coli uses DLDH to convert pyruvate into D-lactate using nicotinamide adenine dinucleotide- hydrogen (NADH) under anaerobic conditions and low pH [1]. Electrons from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, providing energy for active transport of amino acids and sugars across cell membranes [2].

Experiment

This enzyme is implemented in the synthesis pathway to produce salvianic acid A in an E. coli culture. This enzyme converts 4-hydroxyphenylpyruvate into 4-dihydroxy phenyllactate by replacing a carbon double-bonded oxygen with a carbon-bonded hydroxyl group. In the presence of 3,4-dihydroxy phenylpyruvate, DLDH will convert it to salvianic acid A by replacing a carbon double-bonded oxygen with a carbon-bonded hydroxyl group [3].

This part was obtained by DNA synthesis and can be used in a Bio-Safety Level 1 (BLS-1) laboratory.

References

1. Bunch, P. K., Mat-Jan, F., Lee, N., & Clark, D. P. (1997). The ldhA gene encoding the fermentative lactate dehydrogenase of Escherichia coli. Microbiology (Reading, England), 143 ( Pt 1), 187–195. https://doi.org/10.1099/00221287-143-1-187

2. P06149 · DLD_ECOLI. UniProt. (n.d.). https://www.uniprot.org/uniprotkb/P06149/entry

3. Bloch, S. E., & Schmidt‐Dannert, C. (2014). Construction of a chimeric biosynthetic pathway for the de novo biosynthesis of rosmarinic acid in escherichia coli. ChemBioChem, 15(16), 2393–2401. https://doi.org/10.1002/cbic.201402275