Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Naropantul Appaji Rao"'
Publikováno v:
Biochemical Journal. 369:469-476
Serine hydroxymethyltransferase (SHMT), a pyridoxal 5′-phosphate (PLP)-dependent enzyme, catalyses the transfer of the hydroxymethyl group from serine to tetrahydrofolate to yield glycine and N5,N10-methylenetetrahydrofolate. An analysis of the kno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ca81ef3e07de8834f936e6c14962d72
https://doi.org/10.1042/bj20021160
https://doi.org/10.1042/bj20021160
Autor:
Vijayapandian Leelavathy, Jala V. Krishna Rao, Naropantul Appaji Rao, Rashmi Talwar, Handanahal S. Savithri
Publikováno v:
Biochemical Journal. 350:849-853
Serine hydroxymethyltransferase belongs to the α class of pyridoxal-5´-phosphate enzymes along with aspartate aminotransferase. Recent reports on the three-dimensional structure of human liver cytosolic serine hydroxymethyltransferase had suggested
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76d6b4f129a3f9339149385bdc722fc2
https://doi.org/10.1042/bj3500849
https://doi.org/10.1042/bj3500849
Autor:
Handanahal S. Savithri, Naropantul Appaji Rao, Asis Datta, V. Prakash, Junutala R. Jagath, Rashmi Talwar
Publikováno v:
Acta Biochimica Polonica. 44:679-688
The active site lysine residue, K256, involved in Schiff's base linkage with pyridoxal-5'-phosphate (PLP) in sheep liver recombinant serine hydroxymethyltransferase (rSHMT) was changed to glutamine or arginine by site-directed mutagenesis. The purifi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::badfa8f8993c0431ef95fe2a650039d6
https://doi.org/10.18388/abp.1997_4370
https://doi.org/10.18388/abp.1997_4370
Autor:
Naropantul Appaji Rao, J.K. Acharya
Publikováno v:
Journal of Biological Chemistry. 267:19066-19071
An unusual intermediate bound to the enzyme was detected in the interaction of thiosemicarbazide with sheep liver serine hydroxymethyltransferase. This intermediate had absorbance maxima at 464 and 440 nm. Such spectra are characteristic of resonance
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51de633aeaeb4572c605e01fd1f24295
https://doi.org/10.1016/s0021-9258(18)41741-3
https://doi.org/10.1016/s0021-9258(18)41741-3
Publikováno v:
Scopus-Elsevier
Jacalin [Artocarpus integrifolia (jack fruit) agglutinin] is made up of two types of chains, heavy and light, with M(r) values of 16,200 +/- 1200 and 2090 +/- 300 respectively (on the basis of gel-permeation chromatography under denaturing conditions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49ab437d447b6240fbdf29418fc7b5e4
https://doi.org/10.1042/bj2840095
https://doi.org/10.1042/bj2840095
Publikováno v:
Journal of Biological Chemistry. 267:9289-9293
The arginine residue(s) necessary for tetrahydrofolate binding to sheep liver serine hydroxymethyltransferase were located by phenylglyoxal modification. The incorporation of [$7-^{14}C$]phenylglyoxal indicated that 2 arginine residues were modified
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5b799dc4d53fe0e2a0b7b342814ce5ea
https://doi.org/10.1016/s0021-9258(19)50421-5
https://doi.org/10.1016/s0021-9258(19)50421-5
Publikováno v:
The Lens
In an attempt to identify the arginine residue involved in binding of the carboxylate group of serine to mammalian serine hydroxymethyltransferase, a highly conserved Arg-401 was mutated to Ala by site-directed mutagenesis. The mutant enzyme had a ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dd0209e23d9b46267df32bae9a35ea1e
http://eprints.iisc.ac.in/24694/1/4.pdf
http://eprints.iisc.ac.in/24694/1/4.pdf
Publikováno v:
IndraStra Global.
In an attempt to unravel the role of conserved histidine residues in the structure-function of sheep liver cytosolic serine hydroxymethyltransferase (SHMT), three site-specific mutants (H134N, H147N, and H150N) were constructed and expressed, H134N a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9aafb4bc920f72966ad3e28978e5ba43
https://igi.indrastra.com/items/show/193349
https://igi.indrastra.com/items/show/193349
Publikováno v:
European journal of biochemistry. 230(2)
A sheep liver cDNA clone for the cytosolic serine hydroxymethyltransferase (SHMT) was isolated and its nucleotide sequence determined. The full-length cDNA of SHMT was placed under the control of T7 promoter in pET-3C plasmid and expressed in Escheri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bafb9af03b1b9ffc4743e66d35c72144
https://pubmed.ncbi.nlm.nih.gov/7607226
https://pubmed.ncbi.nlm.nih.gov/7607226
Publikováno v:
Journal of Biological Chemistry. 264:6273-6279
The coat protein of belladonna mottle virus (a tymovirus) was cleaved by trypsin and chymotrypsin, and the peptides were separated by high performance liquid chromatography using a combination of gel permeation, reverse phase, and ion pair chromatogr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bb55eb1e28952bd7e4df96cdc71ef2ec
https://doi.org/10.1016/s0021-9258(18)83344-0
https://doi.org/10.1016/s0021-9258(18)83344-0