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Origin of the Allyl Group in FK506 Biosynthesis*
- D. Goranovič, G. Kosec, +5 authors H. Petković
- Biology, MedicineThe Journal of Biological Chemistry
- 1 March 2010
A biosynthetic pathway for the provision of an unusual five-carbon extender unit, which is carried out by a novel diketide synthase complex is proposed.
Novel chemobiosynthetic approach for exclusive production of FK506.
Using a combination of metabolic engineering and chemobiosynthetic approach, the exclusive production of FK506 is achieved, representing a significant step towards development of an advanced industrial bioprocess.
FK506 biosynthesis is regulated by two positive regulatory elements in Streptomyces tsukubaensis
The results clearly demonstrate the positive regulatory role of fkbR and fkbN genes in FK506 biosynthesis in S. tsukubaensis NRRL 18488 and show that regulatory mechanisms can differ substantially from other, even apparently closely similar Fk506-producing strains, reported in literature.
Cathepsin S in tumours, regional lymph nodes and sera of patients with lung cancer: relation to prognosis
Evidence that Cat S may be involved in malignant progression is provided and its role differs from that of the related Cats B and L and could be associated with the immune response rather than with remodelling of extracellular matrix.
Molecular cloning and immunocytochemical localization of jasmonic acid inducible cathepsin D inhibitors from potato.
- B. Strukelj, M. Ravnikar, +5 authors V. Turk
- Chemistry, MedicineAdvances in experimental medicine and biology
The protein sequences of two closely related isoinhibitors, PDI and NID, isolated from potato tubers, were determined.
Molecular cloning of a putative homolog of proline/arginine‐rich antibacterial peptides from porcine bone marrow
Screening of a porcine bone marrow cDNA library with a PCR‐derived probe from rabbit LPS‐binding protein CAP18 led to the discovery of two closely related clones that have a novel, unique structure of the C‐terminal region of 100 amino acid residues with a repeating sequence often residues (FPPPNXPGPR, where X = V or F).
Folding and activation of human procathepsin S from inclusion bodies produced in Escherichia coli.
- G. Kopitar, M. Dolinar, B. Strukelj, J. Pungercar, V. Turk
- Chemistry, MedicineEuropean journal of biochemistry
- 1 March 1996
The recombinant cathepsin S was catalytically active on fluorogenic substrates and had kinetic properties similar to those of recombinant enzyme produced in yeast.
Molecular cloning and identification of a novel porcine cathelin-like antibacterial peptide precursor.
- B. Strukelj, J. Pungercar, +4 authors V. Turk
- Chemistry, MedicineBiological chemistry Hoppe-Seyler
- 1 August 1995
A novel clone (C6) encoding the precursor of a 79-residue proline/arginine-rich antibacterial peptide prophenin was isolated from a porcine bone marrow cDNA library. Its deduced N-terminal propart…
A Highly Productive, Whole-Cell DERA Chemoenzymatic Process for Production of Key Lactonized Side-Chain Intermediates in Statin Synthesis
- Matej Ošlaj, J. Cluzeau, Damir Orkič, G. Kopitar, P. Mrak, Zdenko Časar
- Chemistry, MedicinePloS one
- 7 May 2013
To the authors' knowledge, this is the first asymmetric aldol condensation process achieved with whole-cell DERA catalysis and it simplifies and extends previously developed DERA-catalyzed approaches based on the isolated enzyme.
Refolding of recombinant sulphonated procathepsin S and of reduced chicken cystatin; implications for renaturation experiments.
- E. Žerovnik, G. Kopitar, J. Kos, V. Turk
- Chemistry, MedicineBiochimica et biophysica acta
- 2 April 1998
Kinetic stopped-flow measurements of refolding of the recombinant sulphonated procathepsin S from 6 M urea are presented, showing a late, 'more structured' intermediate which is prone to dimerization.