Biochimica et Biophysica Acta (BBA) - Enzymology最新文献

Study on the role of tyrosine side-chains at the active centre of emulsin β-d-glucosidase 乳化剂β-d-葡萄糖苷酶活性中心酪氨酸侧链作用的研究

Biochimica et Biophysica Acta (BBA) - Enzymology Pub Date : 1981-12-15 DOI: 10.1016/0005-2744(81)90043-7

László Kiss, Ibolya Kóródi, Pál Nánási

引用次数: 4

Titles of related papers in other sections 其他章节相关论文的标题

Biochimica et Biophysica Acta (BBA) - Enzymology Pub Date : 1981-12-15 DOI: 10.1016/0005-2744(81)90046-2

引用次数: 0

Essential histidine residues of ribulosebisphosphate carboxylase indicated by reaction with diethylpyrocarbonate and rose bengal 核酮糖二磷酸羧化酶必需组氨酸残基与焦碳酸二乙酯和孟加拉玫瑰的反应

Biochimica et Biophysica Acta (BBA) - Enzymology Pub Date : 1981-12-15 DOI: 10.1016/0005-2744(81)90028-0

A.S. Bhagwat, J. Ramakrishna

{"title":"Essential histidine residues of ribulosebisphosphate carboxylase indicated by reaction with diethylpyrocarbonate and rose bengal","authors":"A.S. Bhagwat, J. Ramakrishna","doi":"10.1016/0005-2744(81)90028-0","DOIUrl":"10.1016/0005-2744(81)90028-0","url":null,"abstract":"<div>Modification of ribulosebisphosphate carboxylase (3-phospho-d-glycerate carboxy-lyase (dimerizing), EC 4.1.1.39) by diethylpyrocarbonate or rose bengal-sensitized photooxidation caused rapid inactivation of the enzyme. The photooxidation proceeded following pseudo-first-order reaction kinetics showing a maximal value at pH 8.0. The fully activated enzyme was more sensitive to photooxidation as compared to the unactivated enzyme. The enzyme partially inactivated by photooxidation was fully sensitive to the positive effectors. The photooxidised enzyme showed a characteristic increase in absorbance at 250 nm which was dependent on the extent of inactivation. The kinetic analyses and correlation of the spectral changes with the activity indicated that the inactivation by diethylpyrocarbonate resulted from the modification of an average one histidine residue/70 000-dalton combination of large and small subunit. Sulfhydryl, lysine and tyrosine residues were not modified by diethylpyrocarbonate treatment. Ribulosebisphosphate and some effectors of the enzyme offered significant protection against diethylpyrocarbonate modification indicating that diethylpyrocarbonate was interacting with the enzyme at or near the active site.</div>","PeriodicalId":100159,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2744(81)90028-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86971724","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 15

Partial characterization and studies of fibroblast and leucocyte neuraminidase activities towards sialyloligosaccharides in adult sialidosis and mucolipidosis II and III 成纤维细胞和白细胞神经氨酸酶对唾液寡糖在成人唾液病和粘脂病II和III中的活性的部分表征和研究

Biochimica et Biophysica Acta (BBA) - Enzymology Pub Date : 1981-12-15 DOI: 10.1016/0005-2744(81)90033-4

Masaru Kuriyama , Futaba Someya , Tadashi Miyatake , Masai Koseki

{"title":"Partial characterization and studies of fibroblast and leucocyte neuraminidase activities towards sialyloligosaccharides in adult sialidosis and mucolipidosis II and III","authors":"Masaru Kuriyama , Futaba Someya , Tadashi Miyatake , Masai Koseki","doi":"10.1016/0005-2744(81)90033-4","DOIUrl":"10.1016/0005-2744(81)90033-4","url":null,"abstract":"<div>We described the partial characterization and some properties of fibroblast and leucocyte neuraminidase towards 2 → 3 and 2 → 6 sialyllactose, and 2 → 3 and 2 → 6 sialylhexasaccharide which were isolated from the urine of a patient with adult sialidosis with partial β-galactosidase deficiency. Neuraminidase activities were assayed using the radioactive-labeled derivatives of these saccharide substrates. These neuraminidases (acylneuraminyl hydrolase, EC 3.2.1.18) were partially inactivated by homogenization, sonication and freeze-thawing treatment. The leucocyte neuraminidase was more labile than that of fibroblasts. Fibroblast neuraminidase had about a 10-fold higher activity than leucocyte neuraminidase towards the respective substrates. The neuraminidase from fibroblasts and leucocytes were each able to hydrolyze 2 → 3 isomers 2–3-times faster than 2 → 6 isomers and the sialyllactoses 1.5–3.0-times faster than sialylhexasaccharides. Neuraminidase activities towards all four substrates were deficient in fibroblasts and leucocytes from the patients with adult sialidosis. Loss of activity was especially prominent in fibroblasts, while considerable residual activities (about 20–30%) remained in leucocytes. In mucolipidosis II and III patients, these neuraminidase activities showed normal levels in leucocytes, although they were decreased in fibroblasts. The discrepancy between neuraminidase activities towards 2 → 3 and 2 → 6 isomers was not found in all the cases.</div>","PeriodicalId":100159,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2744(81)90033-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18330379","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 4

The kinetics of unphosphorylated, phosphorylated and proteolytically modified fructose bisphosphatase from rat liver 大鼠肝脏中未磷酸化、磷酸化和蛋白水解修饰果糖双磷酸酶的动力学

Biochimica et Biophysica Acta (BBA) - Enzymology Pub Date : 1981-12-15 DOI: 10.1016/0005-2744(81)90038-3

Pia Ekman, Ulla Dahlqvist-Edberg

{"title":"The kinetics of unphosphorylated, phosphorylated and proteolytically modified fructose bisphosphatase from rat liver","authors":"Pia Ekman, Ulla Dahlqvist-Edberg","doi":"10.1016/0005-2744(81)90038-3","DOIUrl":"10.1016/0005-2744(81)90038-3","url":null,"abstract":"<div>Phosphorylation of fructose-bisphosphatase (d-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) by the catalytic subunit of cyclic AMP-dependent protein kinase from pig muscle decreased the K0.5 for fructose-bisphosphate from 21 to 11 μM. When the phosphorylated fructose-bisphosphatase was treated with trypsin the K0.5 increased to 22 μM. The K0.5 also increased when the phosphoenzyme was treated with a partially purified phosphatase from rat liver. There was no difference between the unphosphorylated and phosphorylated enzyme with respect to pH dependence, the pH optimum being about 7.0 for both. Limited treatment of fructose-bisphosphatase with subtilisin, which cleaves the enzyme at its unphosphorylatable N-terminal part, increased the pH optimum more than limited treatment with trypsin, which releases the phosphorylated peptide at the C-terminal part of fructose-bisphosphatase. The phosphorylated site on the phosphorylated fructose-bisphosphatase was more easily split off by trypsin treatment than the corresponding unphosphorylated site. The results suggest in addition to the glucagon-induced phosphorylation of fructose-bisphosphatase described by Claus et al. [1] that the phosphorylation-dephosphorylation of fructose-bisphosphatase could be of importance for the hormonal regulation of the enzyme in vivo.</div>","PeriodicalId":100159,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2744(81)90038-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17336852","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 19

Porcine thyroid fucosidase 猪甲状腺聚焦酶

Biochimica et Biophysica Acta (BBA) - Enzymology Pub Date : 1981-12-15 DOI: 10.1016/0005-2744(81)90036-X

Deborah Shuey Grove , George S. Serif

引用次数: 17

A differential labeling model for determining the number of catalytically essential carboxyl groups in fumarase 确定延胡索酶中催化必需羧基数量的微分标记模型

Biochimica et Biophysica Acta (BBA) - Enzymology Pub Date : 1981-12-15 DOI: 10.1016/0005-2744(81)90030-9

Robert C. Seid Jr. , Thomas P. Sakmar

引用次数: 0

Biosynthesis of riboflavin 核黄素的生物合成

Biochimica et Biophysica Acta (BBA) - Enzymology Pub Date : 1981-12-15 DOI: 10.1016/0005-2744(81)90044-9

Peter Nielsen, Adelbert Bacher

引用次数: 38

Differential effects of the NADPH/NADP+ ratio on the activities of hexose-6-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase NADPH/NADP+比值对己糖-6-磷酸脱氢酶和葡萄糖-6-磷酸脱氢酶活性的差异影响

Biochimica et Biophysica Acta (BBA) - Enzymology Pub Date : 1981-12-15 DOI: 10.1016/0005-2744(81)90045-0

Koh-Ichi Oka, Takayuki Takahashi , Samuel H. Hori

{"title":"Differential effects of the NADPH/NADP+ ratio on the activities of hexose-6-phosphate dehydrogenase and glucose-6-phosphate dehydrogenase","authors":"Koh-Ichi Oka, Takayuki Takahashi , Samuel H. Hori","doi":"10.1016/0005-2744(81)90045-0","DOIUrl":"10.1016/0005-2744(81)90045-0","url":null,"abstract":"<div>The steady-state kinetics of rat liver hexose-6-phosphate dehydrogenase (β-d-glucose: NAD(P)+ 1-oxidoreductase, EC 1.1.1.47) using glucose 6-phosphate and NADP+ as substrates is studied. NADPH has been found to inhibit the enzyme noncompetitively with respect to NADP+, and uncompetitively with respect to glucose 6-phosphate. At a given concentration of glucose 6-phosphate, the reaction follows the basic inhibition equation. This suggests the presence of the enzyme-NADP+-NADPH complex, and contrasts with the NADPH inhibition of glucose-6-phosphate dehydrogenase which is competitive with respect to NADP+. An attempt was made to estimate the in vivo activities of the two enzymes in rat liver in the presence of NADPH at various NADPH/NADP+ ratios. The results show that the two enzymes appear to be at about the same level of activity in normal rat liver where the coenzyme redox ratio is 110 and the glucose 6-phosphate concentration is 217 μM. Under the same conditions, but with 50 μM dehydroepiandrosterone, a potent inhibitor of glucose-6-phosphate dehydrogenase, but not of hexose-6-phosphate dehydrogenase, the latter enzyme is estimated to be 1.6-times as active as the former. Such differential effects of NADPH and steroids on the two enzymes may support our notion that hexose-6-phosphate dehydrogenase may have advantages over glucose-6-phosphate dehydrogenase (d-glucose-6-phosphate: NADP+ 1-oxidoreductase, EC 1.1.1.49) in steroid-metabolizing tissues (the activity of hexose-6-phosphate dehydrogenase is not, or less, affected by steroids or NADPH).</div>","PeriodicalId":100159,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2744(81)90045-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18330385","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 18

Tripeptidyl carboxypeptidase activity of kininase II (angiotensin-converting enzyme) 三肽基羧基肽酶活性(血管紧张素转换酶)

Biochimica et Biophysica Acta (BBA) - Enzymology Pub Date : 1981-12-15 DOI: 10.1016/0005-2744(81)90042-5

Jin-Ichi Inokuchi, Atsuo Nagamatsu

{"title":"Tripeptidyl carboxypeptidase activity of kininase II (angiotensin-converting enzyme)","authors":"Jin-Ichi Inokuchi, Atsuo Nagamatsu","doi":"10.1016/0005-2744(81)90042-5","DOIUrl":"10.1016/0005-2744(81)90042-5","url":null,"abstract":"<div>The degradation of des-Arg9-bradykinin and its analogues by highly purified preparations of hog lung and kidney kininase II (angiotensin-converting enzyme; peptidyldipeptide hydrolase, EC 3.4.15.1) was studied. The degradative peptide fragments were separated and isolated by high performance liquid chromatography and identified by amino acid analysis. Both enzymes released C-terminal tripeptides from des-Arg9-bradykinin, des-Arg9-(Leu8)-bradykinin, Pro-Pro-Gly-Phe-Ser-Pro-Phe, Pro-Gly-Phe-Ser-Pro-Phe, Gly-Phe-Ser-Pro-Phe, Bz-Gly-Ser-Pro-Phe and Bz-Gly-Ala-Pro-Phe. Hydrolysis of Phe-Ser-Pro-Phe, Bz-Gly-His-Pro-Phe, Bz-Gly-Phe-Pro-Phe and Bz-Gly-Gly-Pro-Phe by both enzymes was negligible. These data indicate that kininase II can release C-terminal tripeptides of substrates having a proline residue in the penultimate position such as des-Arg9-bradykinin and its analogues, and that this enzyme is able not only to act as a dipeptidyl carboxypeptidase but also acts as a tripeptidyl carboxypeptidase. The tripeptidyl carboxypeptidase activity of this enzyme was sensitive to inhibition by kininase II inhibitors.</div>","PeriodicalId":100159,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1981-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2744(81)90042-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"17336853","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 47