Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Takayuki Nishijyo"'
Autor:
Stephan Heeb, Yoshifumi Itoh, Takayuki Nishijyo, Ursula Schnider, Christoph Keel, Julie Wade, Ultan Walsh, Fergal O'Gara, Dieter Haas
Publikováno v:
Molecular Plant-Microbe Interactions, Vol 13, Iss 2, Pp 232-237 (2000)
The minimal replicon of the Pseudomonas plasmid pVS1 was genetically defined and combined with the Escherichia coli p15A replicon, to provide a series of new, oligocopy cloning vectors (5.3 to 8.3 kb). Recombinant plasmids derived from these vectors
Externí odkaz:
https://doaj.org/article/f88050c3ab0748eab7b2f75ed453f605
Publikováno v:
Journal of Bacteriology. 184:5633-5640
Pseudomonas aeruginosa PAO1 utilizes proline as the sole source of carbon and nitrogen via a bifunctional enzyme (the putA gene product) that has both proline dehydrogenase (EC 1.5.99.8) and pyrroline 5-carboxylate dehydrogenase (EC 1.5.1.12) activit
Publikováno v:
Journal of Bacteriology. 183:6517-6524
Pseudomonas aeruginosa PAO1 utilizes agmatine as the sole carbon and nitrogen source via two reactions catalyzed successively by agmatine deiminase (encoded by aguA ; also called agmatine iminohydrolase) and N -carbamoylputrescine amidohydrolase (enc
Publikováno v:
Molecular Microbiology. 40:917-931
A novel two-component system, CbrA-CbrB, was discovered in Pseudomonas aeruginosa; cbrA and cbrB mutants of strain PAO were found to be unable to use several amino acids (such as arginine, histidine and proline), polyamines and agmatine as sole carbo
Autor:
U. F. Walsh, Yoshifumi Itoh, Dieter Haas, Ursula Schnider, Christoph Keel, Julie Wade, Takayuki Nishijyo, Stephan Heeb, Fergal O'Gara
Publikováno v:
Molecular Plant-Microbe Interactions®. 13:232-237
The minimal replicon of the Pseudomonas plasmid pVS1 was genetically defined and combined with the Escherichia coli p15A replicon, to provide a series of new, oligocopy cloning vectors (5.3 to 8.3 kb). Recombinant plasmids derived from these vectors
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1386:227-232
We isolated a new clone that showed structural similarities with the rat peptidylarginine deiminase (PAD) types II and III. The full-length cDNA sequence of this novel PAD comprised 1998 bp encoding a sequence for 666 amino acid residues (Mr 74 467),
Publikováno v:
Journal of bacteriology. 180(21)
The complete nucleotide sequence for the aot operon of Pseudomonas aeruginosa PAO1 was determined. This operon contains six open reading frames. The derived sequences for four of these, aotJ , aotQ , aotM , and aotP , show high similarity to those of
Publikováno v:
Journal of biochemistry. 121(5)
Peptidylarginine deiminase (PAD) is a post-translational modification enzyme that catalyzes deimination of arginine residues of proteins in the presence of calcium ions. There are three types of PAD in rodent tissues: PAD types I, II, and III [Teraka