Analysis of glutamines in catalysis in Cephalosporium acremonium isopenicillin N synthase by site-directed mutagenesis

Analysis of glutamines in catalysis in Cephalosporium acremonium isopenicillin N synthase by site-directed mutagenesis

10.1006/bbrc.1998.9663

محفوظ في:

التفاصيل البيبلوغرافية
المؤلفون الرئيسيون:	Loke, P., Tiow Suan Sim
مؤلفون آخرون:	MICROBIOLOGY
التنسيق:	مقال
منشور في:	2012
الموضوعات:	Cephalosporium acremonium Glutamine Isopenicillin N synthase Site-directed mutagenesis
الوصول للمادة أونلاين:	http://scholarbank.nus.edu.sg/handle/10635/31032
الوسوم:	إضافة وسم لا توجد وسوم, كن أول من يضع وسما على هذه التسجيلة!

مواد مشابهة

Catalytic activity in cephalosporium acremonium isopenicillin N synthase does not involve glutamine-234
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منشور في: (2012)

Analysis of a conserved arginine R281L in catalysis in Cephalosporium acremonium isopenicillin N synthase
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Mutational evidence for the role of serine-283 in Cephalosporium acremonium isopenicillin N synthase
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Functional analysis of a conserved aspartate D218 in Cephalosporium acremonium isopenicillin N synthase
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Mutational analysis of conserved glycines 42 and 256 in Cephalosporium acremonium isopenicillin N synthase
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Site-directed mutagenesis of arginine-89 supports the role of its guanidino side-chain in substrate binding by Cephalosporium acremonium isopenicillin N synthase
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Histidine-272 of isopenicillin N synthase of Cephalosporium acremonium, which is possibly involved in iron binding, is essential for its catalytic activity
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Mutational analysis of tyrosine-191 in the catalysis of Cephalosporium acremonium isopenicillin N synthase
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Site-Directed Mutagenesis of Proline-285 to Leucine in Cephalosporium acremonium Isopenicillin N - Synthase Affects Catalysis and Increases Soluble Expression at Higher Temperatures
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Replacement of tyrosine-197 and the corresponding tyrosine-195 to isoleucine in Cephalosporium acremonium and Streptomyces clavuligerus isopenicillin N synthase
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Glutamine-230 influences enzyme solubility but not catalysis in Streptomyces clavuligerus isopenicillin N synthase
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Involvement of a third histidine in the ferrous active site of isopenicillin N synthase of Cephalosporium acremonium repudiated by recombinant double histidine mutants
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A comparison of three site-directed mutagenesis kits
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Construction of Streptomyces jumonjinensis isopenicillin N synthase double mutants, Ser119Ala/Glu120Gly and Thr308Ala/Thr309Val, overcomes insoluble expression in Escherichia coli
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C-terminus modification of Streptomyces clavuligerus deacetoxycephalosporin C synthase improves catalysis with an expanded substrate specificity
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