نتایج جستجو برای: pectin lyase enzyme

تعداد نتایج: 252689  

Journal: :The Biochemical journal 1952
W W REID

It was reported by Beavan & Brown (1949) that cultures of By8aochlamy8 fulva Olliver & Smith produced protopectinase, but neither polygalacturonase nor pectin esterase; they concluded that B. fulva produced a disaggregating enzyme, which lowered the viscosity ofpectin solutions, without the formation of free reducing groups. A re-investigation of the problem has been made, and in a preliminary ...

Journal: :Microbiology and molecular biology reviews : MMBR 2008
D Wade Abbott Alisdair B Boraston

SUMMARY Pectin is a structural polysaccharide that is integral for the stability of plant cell walls. During soft rot infection, secreted virulence factors from pectinolytic bacteria such as Erwinia spp. degrade pectin, resulting in characteristic plant cell necrosis and tissue maceration. Catabolism of pectin and its breakdown products by pectinolytic bacteria occurs within distinct cellular e...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1984
J Knappe F A Neugebauer H P Blaschkowski M Gänzler

Pyruvate formate-lyase (formate acetyltransferase; EC 2.3.1.54) of Escherichia coli cells is post-translationally interconverted between inactive and active forms. Conversion of the inactive to the active form is catalyzed by an Fe2+-dependent activating enzyme and requires adenosylmethionine and dihydroflavodoxin. This process is shown here to introduce a paramagnetic moiety into the structure...

Journal: :The Journal of biological chemistry 1990
N A Elshourbagy J C Near P J Kmetz G M Sathe C Southan J E Strickler M Gross J F Young T N Wells P H Groot

ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. We have isolated a full-length cDNA copy of 4.3 kilobase pairs encoding the ATP-citrate lyase mRNA by screening rat liver cDNA library using oligonucleotide probes designed from peptide sequences obtained from the purified rat enzyme. Expression of this cDNA in bacteria, followed by im...

2006
Rong - sen Shen Richard R. Fritz Creed W. Abell

Yeast phenylalanine ammonia-lyase was administered i.p. to normal and tumor-beaning mice, and its clearance from plasma was studied. Single and multiple weekly injections at dosages of 10, 20, 50, and 100 units/kg were adminis tered to C57BL female, C57BL x DBA/2 F male, and A/J female mice. L5178Y munine lymphoblastic leukemia, B16 melanoma, BW10232 adenocancinoma, and 15091A ana plastic carci...

Journal: :The Biochemical journal 1989
H G Nimmo F Douglas C Kleanthous D G Campbell C MacKintosh

Escherichia coli isocitrate lyase was inactivated by iodacetate in a pseudo-first-order process. Complete inactivation was associated with the incorporation of only one carboxymethyl group per enzyme subunit. The substrate and products of the enzyme protected against inactivation, suggesting that the reactive group may be located at the active site. Isolation and sequencing of a carboxymethylat...

Journal: :Journal of biochemistry and molecular biology 2004
Wan-Seok Kim Byung-Taek Kim Dong-Hyun Kim Yeong Shik Kim

Heparin lyase I was purified to homogeneity from Bacteroides stercoris HJ-15 isolated from human intestine, by a combination of DEAE-Sepharose, gel-filtration, hydroxyapatite, and CM-Sephadex C-50 column chromatography. This enzyme preferred heparin to heparan sulfate, but was inactive at cleaving acharan sulfate. The apparent molecular mass of heparin lyase I was estimated as 48,000 daltons by...

2013
Marie E Beckner

Other names: ACL, ATPCL, CLATP HGNC (Hugo): ACLY Location: 17q21.2 Note Note that the International Union for Biochemistry and Molecular Biology (IUBMB)'s enzyme nomenclature accepts ATP citrate synthase as the name for ACLY's encoded protein (EC 2.3.3.8). However, ATP citrate lyase is more commonly used and other names include citrate cleavage enzyme, ATP-citrate (pro-S)-lyase, ATPCL, CLATP. A...

Journal: :The Journal of biological chemistry 1969
R O Brady C Borek R M Bradley

The dehydroalanine present in histidine ammonia lyase is essential for the activity of this enzyme, and may be at the active site. This was shown by recovery of 3H-alanine4 and loss of activity on reduction of the enzyme with NaBaH4, and by protection of both reduction and inactivation by histidine. Since several pyruvate-containing enzymes have been described recently (1P17), it is important t...

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