Phosphoglycolate Phosphatase
Author : John Tane Christeller
Publisher :
Page : 486 pages
File Size : 11,63 MB
Release : 1974
Category : Chloroplasts
ISBN :
Author : John Tane Christeller
Publisher :
Page : 486 pages
File Size : 11,63 MB
Release : 1974
Category : Chloroplasts
ISBN :
Author : Mary Joyce Abbate
Publisher :
Page : 252 pages
File Size : 46,98 MB
Release : 1971
Category : Phosphatases
ISBN :
Author : Daria Marie Engelmann
Publisher :
Page : 0 pages
File Size : 24,14 MB
Release : 2023
Category :
ISBN :
Author : Daria Marie Engelmann
Publisher :
Page : 0 pages
File Size : 29,27 MB
Release : 2019
Category :
ISBN :
Author : Regina A. Puts
Publisher :
Page : 120 pages
File Size : 19,97 MB
Release : 2010
Category : Phosphatases
ISBN :
"The function of phosphoglycolate phosphatase (PGPase) in photosynthetic organisms such as green algae (Chlamydomonas reinhardti) is to recycle the 2-phosphoglycolate that is formed as a by-product of the Calvin cycle. The role of PGPase in nonphotosynthetic organisms is less understood, but one potential role that has been suggested is to remove the 2-phosphoglycolate that is formed as a result of DNA repair. This may be the biological role of PHO13 PGPase in Saccharomyces cerevisiae as well. PHO13 PGPase from S. cerevisiae is a member of the PGPase subfamily within the p-nitrophenylphosphatase (p-NPPase) family, which is within the Haloalkanoic Acid Dehalogenase (HAD) superfamily. PHO13 has been subcloned into pET19b to create PHO13(His·Tag). PHO13(HT) was overexpressed and found to be soluble. It purified well by Ni2+-NTA affinity chromatography followed by size-exclusion chromatography. Its expression, solubility, and activity appeared comparable to the native PHO13, but PHO13(HT) was easier to purify due to the histidine tag. Both enzymes had comparable specific activities for both p-nitrophenylphosphate (p-NPP) and 2-phosphoglycolate (PG), pH optima around pH 8.0, optimal activity with >/= 7 mM Mg2+, activity with Co2+ and Mn2+, negligible activity in the presence of Zn2+, and no activity for Ca2+. PHO13(HT) is now ready for x-ray crystal structure determination with our collaborator, Joseph Wedekind, at the University of Rochester."--Abstract.
Author : Isreal Moreno
Publisher :
Page : 150 pages
File Size : 13,90 MB
Release : 2016
Category : Phosphatases
ISBN :
"Staphylococcus aureus is a major cause of hospital-acquired infections. The multi-drug resistant nature of certain S. aureus strains makes the discovery of new drug targets for S. aureus vital. A newly discovered virulence factor from S. aureus was described as an ortholog of NagD from E. coli, a member of the nitrophenyl phosphatase family of the HAD (Haloacid Dehalogenase) superfamily. This thesis will show that this virulence factor is not an ortholog of NagD UMPase from E. coli, but rather a phosphoglycolate phosphatase (PGPase). If phosphoglycolate accumulates in the cell, it will inhibit the glycolytic enzyme triose phosphate isomerase (TPI). In S. aureus, TPI also serves as an adhesion protein that can bind to host cells; phosphoglycolate would interfere with this adhesion process and thus make it harder for S. aureus to infect host cells. Thus, this S. aureus PGPase may act as a virulence factor by degrading the TPI inhibitor phosphoglycolate. We cloned the gene, expressed and purified the protein, and determined and characterized its activity. We have subcloned this PGPase into a His·Tag vector, purified the protein using nickel affinity and size exclusion chromatography, and characterized enzymatic activity, optimal conditions (substrate, pH, and metal usage), and kinetics."--Abstract.
Author : Gabriela Segerer
Publisher :
Page : pages
File Size : 21,97 MB
Release : 2019
Category : Actin
ISBN :
Author : Dietmar Schomburg
Publisher : Springer Science & Business Media
Page : 528 pages
File Size : 41,56 MB
Release : 2002-11-13
Category : Science
ISBN : 9783540439837
The Springer Handbook of Enzymes provides concise data on some 5,000 enzymes sufficiently well characterized – and here is the second, updated edition. Their application in analytical, synthetic and biotechnology processes as well as in food industry, and for medicinal treatments is added. Data sheets are arranged in their EC-Number sequence. The new edition reflects considerable progress in enzymology: the total material has more than doubled, and the complete 2nd edition consists of 39 volumes plus Synonym Index. Starting in 2009, all newly classified enzymes are treated in Supplement Volumes.
Author : William Duncan Patterson Stewart
Publisher : Univ of California Press
Page : 1020 pages
File Size : 21,33 MB
Release : 1974
Category : Science
ISBN : 9780520024106
Author : Daniel L. Purich
Publisher : Elsevier
Page : 551 pages
File Size : 28,64 MB
Release : 2002-11-04
Category : Science
ISBN : 0080489389
The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today—truly an essential publication for researchers in all fields of life sciences. Spectroscopic Detection of Reaction Intermediates Isotopic and Kenetic Detection of Reaction Intermediates Chemical Trapping and Inhibitor Methods for Detecting Reaction Intermediates