Abstract:
:This is the first report describing the enhancement of xylanase activity by the neutral amino acid glycine. Xylanase activity is increased seven-fold at alkaline pH in the presence of glycine and its pH optimum is shifted from pH 7 to 8 without using any protein engineering techniques. Analysis of the steady-state kinetics revealed that glycine in the reaction mixture increases the K(m) and k(cat) values of the enzyme. Chemoaffinity labeling and studies using glycine esters indicate an involvement of the carboxylate ion of glycine in enhancing xylanase catalytic activity. A novel possible mechanism for the glycine-assisted catalytic action of xylanase is proposed.
journal_name
Biol Chemjournal_title
Biological chemistryauthors
Vathipadiekal V,Verma A,Rao Mdoi
10.1515/BC.2007.007subject
Has Abstractpub_date
2007-01-01 00:00:00pages
61-5issue
1eissn
1431-6730issn
1437-4315journal_volume
388pub_type
杂志文章abstract::Meprins are zinc-endopeptidases of the astacin family, which are expressed as membrane-bound or secreted forms in renal and intestinal brush-border membranes of mouse, rat and man. There are two types of meprin subunits, alpha and beta, which form disulfide-bonded homo- and heterodimers; further oligomerization is med...
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journal_title:Biological chemistry
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pub_type: 评论,杂志文章
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journal_title:Biological chemistry
pub_type: 杂志文章
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更新日期:2004-08-01 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章,评审
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更新日期:1997-12-01 00:00:00
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journal_title:Biological chemistry
pub_type: 杂志文章
doi:
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