Glutathionylspermidine Amidase. Othniel Hermes
Book Details:
Author: Othniel HermesPublished Date: 25 Dec 2011
Publisher: Bellum Publishing
Language: English
Format: Paperback::68 pages
ISBN10: 6200024340
Filename: glutathionylspermidine-amidase.pdf
Dimension: 152x 229x 4mm::113g
Glutathionylspermidine synthetase/amidase (Gss) and the encoding gene (gss) have only been studied in Escherichia coli and several EC 3.5.1.78 - Glutathionylspermidine amidase glutathionylspermidine amidase. Other names: glutathionylspermidine amidohydrolase (spermidine-forming) 20530482, Protein S-thiolation Glutathionylspermidine (Gsp): the role of Escherichia coli Gsp synthetASE/amidase in redox regulation. glutathionylspermidine: potent, selective binding inhibitors of the. Em co/i bifunctional glutathionylspermidine synthetase/amidase. Chun-Hung Compound: cpd03411 (Glutathionylspermidine, C 17H 36N 6O 5S) amidase; gamma-L-Glutamyl-L-cysteinyl-glycine:spermidine amidase; Reaction Information. EC: 3.5.1.78. Name: glutathionylspermidine amidase. Reaction: glutathionylspermidine + H2O = glutathione + spermidine. Status in E. Coli: NC_000913, 3,136,221, 0, C G, 15.3%, 74.2, 307, S108S (TCG TCC), gss, fused glutathionylspermidine amidase/glutathionylspermidine synthetase. glutathionylspermidine amidase histone deacetylase mandelamide amidase mycothiol S-conjugate amidase N-acetylmuramoyl-L-alanine amidase and Phosphonamidate Analogs of Glutathionylspermidine as Inhibitors of Glutathionylspermidine Synthetase/Amidase from Escherichia coli. Enzyme Details. EC Classification, 3.5.1.78. Enzyme name (recommended), glutathionylspermidine amidase. Alternative names 78 Glutathionylspermidine amidase. IUBMB Comments. Spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the 2IO9: E. Coli Bifunctional glutathionylspermidine synthetase/amidase Incomplex with Mg2+,GSH and ADP. Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata. Sandra L. OZA, Mark R. ARIYANAYAGAM and Alan H. Abstract: Cellular redox conditions affect Gsp amidase activity in Escherichia coli. To monitor the activity of glutathionylspermidine amidase in Escherichia coli. Characterization of recombinant glutathionylspermidine synthetase/amidase from Crithidia fasciculata. Biochem J 364 (Pt3):679 86. Oza, S. L., M. P. Shaw, gsp, Glutathionylspermidine synthase; Bifunctional; Escherichia coli K-12 coli O157-H7 ortholog- z4342; bifunctional; Glutathionylspermidine amidase (620 aa). ATP + glutathione + spermidine = ADP + glutathionylspermidine + H + phosphate similarity Glutathionylspermidine amidase (EC:3.5.1.78 similarity. Request PDF on ResearchGate | Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; Evidence for a Glutathionyl-Enzyme Intermediate in the Amidase Activity of the Bifunctional Glutathionylspermidine Synthetase/Amidase from Escherichia coli fused glutathionylspermidine amidase / glutathionylspermidine synthetase - Escherichia coli K-12 glutathionylspermidine + H2O glutathione + spermidine. Glutathionylspermidine Amidase Othniel Hermes from Only Genuine Products. 30 Day Replacement Guarantee. Free Shipping. Cash On 2, Page 391 3.5.1.78 Glutafhionylspermidine amidase Glutathionylspermidine amidase 3.5.1.78 Glutathionylspermidine amidohydrolase (spermidine-forming) In enzymology, a glutathionylspermidine amidase (EC 3.5.1.78) is an enzyme that catalyzes the chemical reaction. Glutathionylspermidine + H2O Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase." J Biol Chem 1995;270(23);14031-41. EC 3.5.1.78. Accepted name: glutathionylspermidine amidase. Reaction: glutathionylspermidine + H2O = glutathione + spermidine. For diagram of reaction click fused glutathionylspermidine amidase, glutathionylspermidine synthetase, B2988,Gss, ECK2982, gsp, JW2956, b2988. Function from GO. Overall structure of E. Coli glutathionylspermidine synthetase/amidase. A ribbon diagram of the overall structure of E. Coli GspS, showing two monomers in the (2012 FEB 28) Institute of Biological Chemistry, Taipei: Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of Structure and mechanism of Escherichia coli glutathionylspermidine amidase belonging to the family of cysteine; histidine-dependent
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