Zobrazeno 1 - 10
of 24
pro vyhledávání: '"Irena Pastuszak"'
Publikováno v:
Journal of Biological Chemistry. 285:9803-9812
We show that Mycobacterium smegmatis has an enzyme catalyzing transfer of maltose from [14C]maltose 1-phosphate to glycogen. This enzyme was purified 90-fold from crude extracts and characterized. Maltose transfer required addition of an acceptor. Li
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fb79e2aa137288d44249db870280dcd5
https://doi.org/10.1074/jbc.m109.033944
https://doi.org/10.1074/jbc.m109.033944
Autor:
Alan D. Elbein, J. D. Carroll, Naoki Asano, Vineetha Koroth Edavana, Y. T. Pan, Irena Pastuszak
Publikováno v:
FEBS Journal. 275:3408-3420
Trehalose (α,α-1,1-glucosyl-glucose) is essential for the growth of mycobacteria, and these organisms have three different pathways that can produce trehalose. One pathway involves the enzyme described in the present study, trehalose synthase (TreS
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::029c02675635b3ad9f1bf655e849bc4e
https://doi.org/10.1111/j.1742-4658.2008.06491.x
https://doi.org/10.1111/j.1742-4658.2008.06491.x
Publikováno v:
FEBS Journal. 274:1701-1714
Trehalose is a nonreducing disaccharide of glucose (α,α-1,1-glucosyl-glucose) that is essential for growth and survival of mycobacteria. These organisms have three different biosynthetic pathways to produce trehalose, and mutants devoid of all thre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e92a98ad5436c3ecd41beddb2a77c91c
https://doi.org/10.1111/j.1742-4658.2007.05715.x
https://doi.org/10.1111/j.1742-4658.2007.05715.x
Autor:
Yuan T. Pan, J. David Carroll, Alan D. Elbein, William J. Jourdian, Irena Pastuszak, Vineetha Koroth Edavana, Rick Edmondson
Publikováno v:
European Journal of Biochemistry. 271:4259-4269
Trehalose synthase (TreS) catalyzes the reversible interconversion of trehalose (glucosyl-alpha,alpha-1,1-glucose) and maltose (glucosyl-alpha1-4-glucose). TreS was purified from the cytosol of Mycobacterium smegmatis to give a single protein band on
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e63fe01bb37613de108b8daa2e8a1392
https://doi.org/10.1111/j.1432-1033.2004.04365.x
https://doi.org/10.1111/j.1432-1033.2004.04365.x
Autor:
Vineetha Koroth Edavana, Alan D. Elbein, Prajitha Thampi, Edathera C. Abraham, Irena Pastuszak, J. D. Carroll
Publikováno v:
Archives of Biochemistry and Biophysics. 426:250-257
Two open reading frames in the Mycobacterium tuberculosis genome, Rv3372 and Rv2006 , have about 25% sequence identity at the amino acid level to the trehalose-phosphate phosphatase (TPP) purified from Mycobacterium smegmatis. However, the protein pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e00b783c98987a0ea48e9cac37e39f84
https://doi.org/10.1016/j.abb.2004.02.014
https://doi.org/10.1016/j.abb.2004.02.014
Autor:
Alan D. Elbein, Gary G. Hermanson, Eric R. Sjoberg, Catherine Ketchum, Richard R. Drake, Irena Pastuszak
Publikováno v:
Journal of Biological Chemistry. 273:30165-30174
The enzyme that catalyzes the formation of GDP-l-fucose from GTP and β-l-fucose-1-phosphate (i.e.GDP-β-l-fucose pyrophosphorylase, GFPP) was purified about 560-fold from the cytosolic fraction of pig kidney. At this stage, there were still a number
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a99ef3a2dffacc923476728bd7286b0
https://doi.org/10.1074/jbc.273.46.30165
https://doi.org/10.1074/jbc.273.46.30165
Autor:
Taduesz Szumilo, Halina Szumilo, Alan D. Elbein, Irena Pastuszak, Richard R. Drake, Yucheng Zeng
Publikováno v:
Journal of Biological Chemistry. 271:13147-13154
The pyrophosphorylase that condenses UTP and GlcNAc-1-P was purified 9500-fold to near homogeneity from the soluble fraction of pig liver extracts. At the final stage of purification, the enzyme was quite stable and could be kept for at least 4 month
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::030baff8a75b1bcbfec4ff1c9817c19e
https://doi.org/10.1074/jbc.271.22.13147
https://doi.org/10.1074/jbc.271.22.13147
Publikováno v:
Plant Physiology. 97:396-401
UDP-glucose:dolichylphosphate glucosyltransferase has been purified 734-fold from Triton X-100 solubilized mung bean (Phaseolus aureus) microsomes. The partially purified enzyme has broad pH optima of activity from 6.0 to 7.0 and is maximally stimula
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::61ef2039e912863cfbd8602eef4cbff7
https://doi.org/10.1104/pp.97.1.396
https://doi.org/10.1104/pp.97.1.396
Autor:
Yuan-Tseng, Pan, J D, Carroll, Naoki, Asano, Irena, Pastuszak, Vineetha K, Edavana, Alan D, Elbein
Publikováno v:
The FEBS journal. 275(13)
Trehalose (alpha,alpha-1,1-glucosyl-glucose) is essential for the growth of mycobacteria, and these organisms have three different pathways that can produce trehalose. One pathway involves the enzyme described in the present study, trehalose synthase
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::84724391b542ac490c48203bc51c1e42
https://pubmed.ncbi.nlm.nih.gov/18505459
https://pubmed.ncbi.nlm.nih.gov/18505459
Autor:
Michael L. Mitchell, Gur P. Kaushal, Takaaki Aoyagi, Alan D. Elbein, Russell J. Molyneux, Irena Pastuszak, Joseph E. Tropea
Publikováno v:
Biochemistry. 29:10062-10069
Mannostatin A is a metabolite produced by the microorganism Streptoverticillium verticillus and reported to be a potent competitive inhibitor of rat epididymal {alpha}-mannosidase. When tested against a number of other arylglycosidases, mannostatin A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7958d133bcede89aeddbd064f59c87f7
https://doi.org/10.1021/bi00495a008
https://doi.org/10.1021/bi00495a008