期刊
BIOTECHNOLOGY LETTERS
卷 34, 期 8, 页码 1525-1530出版社
SPRINGER
DOI: 10.1007/s10529-012-0937-0
关键词
Escherichia coli; L-Serine deaminase; L-Serine production; Phosphoglycerate dehydrogenase
资金
- National High-Tech Research and Development Plan (ldquo
- 863rdquo
- Plan) [2011AA100905-4]
- National Natural Science Foundation of China (NSFC) [21076159]
- Program for Changjiang Scholars and innovative Research Team in University (PSCIRT) [IRT1166]
l-Serine is usually produced from glycine. We have genetically engineered Escherichia coli to produce l-serine from glucose intracellularly. d-3-Phosphoglycerate dehydrogenase (PGDH, EC 1.1.1.95) in E. coli catalyzes the first committed step in l-serine formation but is inhibited by l-serine. To overcome this feedback inhibition, both the His(344) and Asn(346) residues of PGDH were converted to alanine and the mutated PGDH (PGDH(dr)) became insensitive to l-serine. However, overexpression of PGDH(dr) gave no significant increase of l-serine accumulation but, when l-serine deaminase genes (sdaA, sdaB and tdcG) were deleted, serine accumulated: (1) deletion of sdaA gave up to 0.03 mmol l-serine/g; (2) deletion of both sdaA and sdaB accumulated l-serine up to 0.09 mmol/g; and (3) deletion of sdaA, sdaB and tdcG gave up to 0.13 mmol l-serine/g cell dry wt.
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