Localization of the factor IX propeptide binding site on recombinant vitamin K dependent carboxylase using benzoylphenylalanine photoaffinity peptide inactivators.
Localization of the factor IX propeptide binding site on recombinant vitamin K dependent carboxylase using benzoylphenylalanine photoaffinity peptide inactivators.
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使用苯甲酰苯丙氨酸光亲和肽灭活剂定位重组维生素 K 依赖性羧化酶上的因子 IX 前肽结合位点。
DOI：
10.1021/bi00002a012
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发表时间：
1995
期刊：
影响因子：
2.9
通讯作者：
Walsh,CT
中科院分区：
文献类型：
--
作者：
Yamada,M;Kuliopulos,A;Nelson,NP;Roth,DA;Furie,B;Furie,BC;Walsh,CT
Revised Manuscript Received October 19, 1994® abstract: The propeptide binding/activation site on the vitamin K dependent carboxylase has been localized to a region of carboxylase between residues Arg+ 50 and Glu+ 225 by photoinactivation studies using [125I] tyrosyl-labeled benzoylphenylalanine (Bpa)-containing analogs of proFIX19, a peptide containing residues—18 to+ 1 of factor IX. Four proFIX19 analogs with Bpa substituents at—16,—13,—7, and—6 were synthesized. These peptides were specific photoinactivators of carboxylase and were used to label a His6-carboxylase construct produced in baculovirus-infected insect cells. Fragments of the labeled carboxylase produced by V8 protease digestion were analyzed by peptide-specific antibodies and by autoradiography. The propeptide recognition site was localized to the N-terminal one-third of the 94 kDa carboxylase. This is consistent with previous studies using a carboxylase substrate affinity label,/V-(bromoacetyl)-FLEELY [Kuliopulos, A., Nelson, N. P., Yamada, M., Walsh, C. T., Furie, B., Furie, B. C., & Roth, D. A.(1994) J. Biol. Chem. 269, 21364—21370], indicating that the propeptidebinding site and the FLEEL binding site are both located within the N-terminal one-third of the vitamin K dependent carboxylase.The vitamin K dependent y-glutamyl carboxylase is a key enzyme in the secretory compartment of liver cells for posttranslational carboxylation of up to 12 glutamyl residues in the first 50 residues of proteins that functionin hemostasis, such as factor IX, factor X, and prothrombin (Furie & Furie, 1988). The posttranslational modification of Glu residues to y-carboxyglutamyl (Gla) 1 residues, generating high-affinity Ca2+ sites, is crucial for the function of these coagulation proteins and their conversion from zymogens to active proteases on membranes (Nelsestuen et al., 1974; Stenflo, 1974; Esmon et al., 1975).
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影响因子：
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作者：
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通讯作者：
Furie,BC
DOI：
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发表时间：
1989
期刊：
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影响因子：
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DOI：
--
发表时间：
1994
期刊：
The Journal of biological chemistry
影响因子：
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作者：
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DOI：
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发表时间：
1993
影响因子：
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作者：
Roth,DA;Rehemtulla,A;Kaufman,RJ;Walsh,CT;Furie,B;Furie,BC
通讯作者：
Furie,BC
影响因子：
15
作者：
S. Gronert;A. Streitwieser
通讯作者：
A. Streitwieser