Found: 9
Select item for more details and to access through your institution.
Biosynthesis of Nylon 12 Monomer, ω-Aminododecanoic Acid Using Artificial Self-Sufficient P450, AlkJ and ω-TA.
- Published in:
- Catalysts (2073-4344), 2018, v. 8, n. 9, p. 400, doi. 10.3390/catal8090400
- By:
- Publication type:
- Article
Biosynthesis of the Nylon 12 Monomer, ω‐Aminododecanoic Acid with Novel CYP153A, AlkJ, and ω‐TA Enzymes.
- Published in:
- Biotechnology Journal, 2018, v. 13, n. 4, p. 1, doi. 10.1002/biot.201700562
- By:
- Publication type:
- Article
Biosynthesis of Medium- to Long-Chain α,ω-Diols from Free Fatty Acids Using CYP153A Monooxygenase, Carboxylic Acid Reductase, and E. coli Endogenous Aldehyde Reductases.
- Published in:
- Catalysts (2073-4344), 2018, v. 8, n. 1, p. 4, doi. 10.3390/catal8010004
- By:
- Publication type:
- Article
Biotransformation of β-keto nitriles to chiral ( S)-β-amino acids using nitrilase and ω-transaminase.
- Published in:
- Biotechnology Letters, 2017, v. 39, n. 4, p. 535, doi. 10.1007/s10529-016-2271-4
- By:
- Publication type:
- Article
Asymmetric synthesis of aromatic β-amino acids using ω-transaminase: Optimizing the lipase concentration to obtain thermodynamically unstable β-keto acids.
- Published in:
- Biotechnology Journal, 2016, v. 11, n. 1, p. 185, doi. 10.1002/biot.201500181
- By:
- Publication type:
- Article
Human Glycolipid Transfer Protein (GLTP) Expression Modulates Cell Shape.
- Published in:
- PLoS ONE, 2011, v. 6, n. 5, p. 1, doi. 10.1371/journal.pone.0019990
- By:
- Publication type:
- Article
Human glycolipid transfer protein (GLTP) genes: organization, transcriptional status and evolution.
- Published in:
- BMC Genomics, 2008, v. 9, p. 1, doi. 10.1186/1471-2164-9-72
- By:
- Publication type:
- Article
Characterization of an oxygen-dependent inducible promoter, the Escherichia coli nar promoter, in gram-negative host strains.
- Published in:
- Biotechnology & Bioengineering, 2003, v. 82, n. 3, p. 271, doi. 10.1002/bit.10567
- By:
- Publication type:
- Article
None of the four tyrosine residues is essential for the biological activity of erythropoietin.
- Published in:
- Archives of Pharmacal Research, 1995, v. 18, n. 6, p. 371, doi. 10.1007/BF02976337
- By:
- Publication type:
- Article