نتایج جستجو برای: pectin lyase enzyme

تعداد نتایج: 252689  

2013
Joel Z. Melnick Paul A. Srere Nabil A. Elshourbagy Orson W. Moe Patricia A. Preisig Robert J. Alpern

Chronic metabolic acidosis increases proximal tubular citrate uptake and metabolism. The present study addressed the effect of chronic metabolic acidosis on a cytosolic enzyme of citrate metabolism, ATP citrate lyase. Chronic metabolic acidosis caused hypocitraturia in rats and increased renal cortical ATP citrate lyase activity by 67% after 7 d. Renal cortical ATP citrate lyase protein abundan...

Journal: :The Journal of clinical investigation 1996
J Z Melnick P A Srere N A Elshourbagy O W Moe P A Preisig R J Alpern

Chronic metabolic acidosis increases proximal tubular citrate uptake and metabolism. The present study addressed the effect of chronic metabolic acidosis on a cytosolic enzyme of citrate metabolism, ATP citrate lyase. Chronic metabolic acidosis caused hypocitraturia in rats and increased renal cortical ATP citrate lyase activity by 67% after 7 d. Renal cortical ATP citrate lyase protein abundan...

Journal: :The Biochemical journal 1996
K M Taylor C P Kaplan X Gao A Baker

Native isocitrate lyase from castor bean and a C-terminally truncated variant were expressed in Saccharomyces cerevisiae under the control of a galactose-inducible promoter. Both forms of isocitrate lyase were targeted to the yeast peroxisomes. They co-fractionated with catalase on sucrose-density-gradient centrifugation of a post-nuclear supernatant prepared from cells grown on oleic acid plus...

Journal: :Journal of bacteriology 1991
J C Hoyt K E Johnson H C Reeves

Acinetobacter calcoaceticus is capable of growing on acetate or compounds that are metabolized to acetate. During adaptation to growth on acetate, A. calcoaceticus B4 exhibits an increase in NADP(+)-isocitrate dehydrogenase and isocitrate lyase activities. In contrast, during adaptation to growth on acetate, Escherichia coli exhibits a decrease in NADP(+)-isocitrate dehydrogenase activity that ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1991
S Y He M Lindeberg A K Chatterjee A Collmer

The out genes of the enterobacterial plant pathogen Erwinia chrysanthemi are responsible for the efficient extracellular secretion of multiple plant cell wall-degrading enzymes, including four isozymes of pectate lyase, exo-poly-alpha-D-galacturonosidase, pectin methylesterase, and cellulase. Out- mutants of Er. chrysanthemi are unable to export any of these proteins beyond the periplasm and ar...

Journal: :Acta crystallographica. Section D, Biological crystallography 2002
Leonard M Thomas Chuong N Doan Randall L Oliver Marilyn D Yoder

Pectate lyase A is a virulence factor secreted by the plant-pathogenic bacteria Erwinia chrysanthemi. The enzyme cleaves the glycosidic bond of pectate polymers by a calcium-dependent beta-elimination mechanism. The crystal structure of pectate lyase A from E. chrysanthemi EC16 has been determined in two crystal forms, monoclinic C2 to 1.8 A and rhombohedral R3 to 2.1 A. The protein structure i...

Journal: :Journal of plant physiology 2008
Mallory Draye Pierre Van Cutsem

The decrease of strawberry (Fragariaxananassa Duch.) fruit firmness observed during ripening is partly attributed to pectolytic enzymes: polygalacturonases, pectate lyases and pectin methylesterases (PMEs). In this study, PME activity and pectin content and esterification degree were measured in cell walls from ripening fruits. Small green, large green, white, turning, red and over-ripe fruits ...

2011
Yansong Miao Hong-Ye Li Jinbo Shen Junqi Wang Liwen Jiang

Pectins are complex polysaccharides that are essential components of the plant cell wall. In this study, a novel putative Arabidopsis S-adenosyl-L-methionine (SAM)-dependent methyltransferase, termed QUASIMODO 3 (QUA3, At4g00740), has been characterized and it was demonstrated that it is a Golgi-localized, type II integral membrane protein that functions in methylesterification of the pectin ho...

Journal: :The Biochemical journal 1949
E C Slater

containing 1 ml. 15 % glycerol solution, 1-0 ml. 0-1 M-sodium acetate, 0-5 ml. 0-3 M-bicarbonate solution and 0 5 ml. of the enzyme solution. Occurrence of the back reaction would have given rise to an uptake of C02 from the system, but in fact no such uptake was observed. Under these conditions, therefore, no back reaction takes place, so that the incompleteness ofthe de-esterification cannot ...

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