Zobrazeno 1 - 10
of 57
pro vyhledávání: '"Mathur R"'
Autor:
Hatti K; Molecular Biophysics Unit, Indian Institute of Science, Bengaluru, Karnataka 560 012, India., Mathiharan YK; Molecular Biophysics Unit, Indian Institute of Science, Bengaluru, Karnataka 560 012, India., Srinivasan N; Molecular Biophysics Unit, Indian Institute of Science, Bengaluru, Karnataka 560 012, India., Murthy MRN; Molecular Biophysics Unit, Indian Institute of Science, Bengaluru, Karnataka 560 012, India.
Publikováno v:
Acta crystallographica. Section D, Structural biology [Acta Crystallogr D Struct Biol] 2017 Jul 01; Vol. 73 (Pt 7), pp. 609-617. Date of Electronic Publication: 2017 Jun 28.
Publikováno v:
Journal of Structural Biology. 202:118-128
Cellular metabolism of amino acids is controlled by a large number of pyridoxal 5'-phosphate (PLP) dependent enzymes. Diaminopropionate ammonia lyase (DAPAL), a fold type II PLP-dependent enzyme, degrades both the D and L forms of diaminopropionic ac
Publikováno v:
Acta Crystallographica Section D Structural Biology. 73:609-617
The determination of the crystal structure of a mutant protein using phases based on a previously determined crystal structure of the wild-type protein is often a straightforward molecular-replacement protocol. Such a structure determination may be d
Autor:
Tiila Riikka Kiema, Neelanjana Janardan, Mathur R. N. Murthy, R.K. Wierenga, Rajesh K. Harijan
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 71:2479-2493
Thiolases catalyze the degradation and synthesis of 3-ketoacyl-CoA molecules. Here, the crystal structures of a T1-like thiolase (MSM-13 thiolase) fromMycobacterium smegmatisin apo and liganded forms are described. Systematic comparisons of six cryst
Autor:
Pallavi Sabharwal, Mathur R. N. Murthy, J. N. Kalyani, Handanahal S. Savithri, G. Deka, Fathima Benazir Jahangir
Publikováno v:
The FEBS journalReferences. 286(18)
A large number of enzymes depend on the ubiquitous cofactor pyridoxal 5 ` phosphate (PLP) for their activity. Pyridoxal kinase (PLK) is the key enzyme involved in the synthesis of PLP from the three forms of vitamin B-6 via the salvage pathway. In th
Autor:
Mathur R. N. Murthy, Ambika M. V. Murthy, Subashini Mathivanan, Handanahal S. Savithri, Sagar Chittori
Publikováno v:
The Lens
Kinases are ubiquitous enzymes that are pivotal to many biochemical processes. There are contrasting views on the phosphoryl-transfer mechanism in propionate kinase, an enzyme that reversibly transfers a phosphoryl group from propionyl phosphate to A
Publikováno v:
Journal of Structural Biology. 189:238-250
In many organisms ``Universal Stress Proteins'' CUSPS) are induced in response to a variety of environmental stresses. Here we report the structures of two USPs, YnaF and YdaA from Salmonella typhimurium determined at 1.8 angstrom and 2.4 angstrom re
Autor:
Kanagaraj Sekar, Mathur R. N. Murthy, Venkatareddy Dadireddy, Kaushik Hatti, Santosh Kumar Chaudhary, Narayanaswamy Srinivasan, Ansuman Biswas
Publikováno v:
Journal of structural biology. 197(3)
In the recent decades, essential steps of protein structure determination such as phasing by multiple isomorphous replacement and multi wave length anomalous dispersion, molecular replacement, refinement of the structure determined and its validation
Autor:
Paul A.M. Michels, Mikael P Karjalainen, Rajesh K. Harijan, Mathur R. N. Murthy, Rik K. Wierenga, Manfred S. Weiss, Tiila R. Kiema, Neelanjana Janardan
Publikováno v:
Biochemical Journal. 455:119-130
Thiolases are essential CoA-dependent enzymes in lipid metabolism. In the present study we report the crystal structures of trypanosomal and leishmanial SCP2 (sterol carrier protein, type-2)-thiolases. Trypanosomatidae cause various widespread devast
Autor:
Mathur R. N. Murthy, Neelanjana Janardan, Rik K. Wierenga, Handanahal S. Savithri, M. Ithayaraja
Thiolases catalyze the Claisen condensation of two acetyl-CoA molecules to give acetoacetyl-CoA, as well as the reverse degradative reaction. Four genes coding for thiolases or thiolase-like proteins are found in theEscherichia coligenome. In this co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4bb6a2d05dcf49d27973cea04adfba0b
https://europepmc.org/articles/PMC4933003/
https://europepmc.org/articles/PMC4933003/