Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Rao , Appaji N"'
Autor:
Bisht, Shveta, Rajaram, Venkatesan, Bharath, Sakshibeedu R., Kalyani, Josyula Nitya, Khan, Farida, Rao, Appaji N., Savithri, Handanahal S., Murthy, Mathur R.N.
Publikováno v:
In Journal of Biological Chemistry 8 June 2012 287(24):20369-20381
Publikováno v:
IndraStra Global.
Serine hydroxymethyltransferase (SHMT) belongs to the alpha-family of pyridoxal 5'-phosphate-dependent enzymes and catalyzes the reversible conversion of L-Ser and etrahydrofolate to Gly and 5,10-methylene tetrahydrofolate. 5,10-Methylene tetrahydrof
Serine hydroxymethyltransferase (SHMT), a pyridoxal-5'-phosphate (PLP) dependent enzyme catalyzes the interconversion of L-Ser and Gly using tetrahydrofolate as a substrate. The gene encoding for SHMT was amplified by PCR from genomic DNA of Bacillus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::40071b6cae61602e5d3529cdd9fb050d
http://eprints.iisc.ernet.in/12348/
http://eprints.iisc.ernet.in/12348/
The three-dimensional structures of human and rabbit liver cytosolic recombinant serine hydroxymethyltransferases (heSHMT and reSHMT) revealed that E75 and Y83 (numbering according to heSHMT)are probable candidates for proton abstraction and Ca-Cb bo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::c37afecee7a2b64e46dc84d6496d5dbc
http://eprints.iisc.ernet.in/1808/
http://eprints.iisc.ernet.in/1808/
Autor:
Savithri, HS, Murthy, Venkatesha Hs, Baskaran, G, Rao, Appaji N, Kool, D, Edkins, E, Wang, W, Bittles, AH
Publikováno v:
IndraStra Global.
During the course of genome studies in a rural community in the South Indian state of Karnataka, DNA-based investigations and counselling for familial adenomatous polyposis (FAP) were requested via the community physician. The proposita died in 1940
The three-dimensional structures of rabbit and human liver cytosolic serine hydroxymethyltransferase revealed that H231 interacts with the O3' of pyridoxal-5'-phosphate and other residues at the active site such as S203, K257, H357 and R402 (numberin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::52a2830516b0d16d26b8a55fd1b1b2d5
http://eprints.iisc.ernet.in/1793/
http://eprints.iisc.ernet.in/1793/
Publikováno v:
IndraStra Global.
Both serine hydroxymethyltransferase and aspartate aminotransferase belong to the $\alpha$-class of pyridoxal-5'-phosphate (pyridoxalP)-dependent enzymes but exhibit different reaction and substrate specificities. A comparison of the X-ray structure
Publikováno v:
IndraStra Global.
Pseudomonas maltophilia CSV89, a soil bacterium, produces an extracellular biosurfactant, ''Biosur-Pm''. The partially purified product is nondialyzable and chemically composed of 50% protein and 12-15% sugar, which indicates the complex nature of Bi
Publikováno v:
IndraStra Global.
2,3-Dihydroxybenzoic acid decarboxylase, the last enzyme in the fungal metabolism of indole to catechol, catalyzes the non-oxidative decarboxylation of 2,3-dihydroxybenzoic acid to catechol. Unlike most other decarboxylases, this enzyme does not requ
Publikováno v:
IndraStra Global.
Serine hydroxymethyltransferase from mammalian and bacterial sources is a pyridoxal-5'-phosphate-containing enzyme, but the requirement of pyridoxal-5'-phosphate for the activity of the enzyme from plant sources is not clear. The specific activity of