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The enzymatic synthesis of dihydrofolate and dihydropteroate in cell-free preparations from wild-type and sulfonamide-resistant pneumococcus.

作者信息

Ortiz P J, Hotchkiss R D

出版信息

Biochemistry. 1966 Jan;5(1):67-74. doi: 10.1021/bi00865a010.

DOI:10.1021/bi00865a010
PMID:4380073
Abstract
摘要

相似文献

1
The enzymatic synthesis of dihydrofolate and dihydropteroate in cell-free preparations from wild-type and sulfonamide-resistant pneumococcus.野生型和磺胺耐药性肺炎球菌无细胞制剂中二氢叶酸和二氢蝶酸的酶促合成。
Biochemistry. 1966 Jan;5(1):67-74. doi: 10.1021/bi00865a010.
2
Dihydrofolate and dihydropteroate synthesis by partially purified enzynes from wild-type and sulfonamide-resistant pneumonococcus.来自野生型和磺胺耐药肺炎球菌的部分纯化酶合成二氢叶酸和二氢蝶酸。
Biochemistry. 1970 Jan 20;9(2):355-61. doi: 10.1021/bi00804a024.
3
The enzymic synthesis of dihydropteroate and dihydrofolate by Plasmodium berghei.伯氏疟原虫对二氢蝶酸和二氢叶酸的酶促合成。
J Protozool. 1973 Aug;20(3):459-64. doi: 10.1111/j.1550-7408.1973.tb00926.x.
4
Rhizopterin biosynthesis in Staphylococcus epidermidis.
Can J Microbiol. 1968 Sep;14(9):933-40. doi: 10.1139/m68-156.
5
The biosynthesis of pteridines.蝶啶的生物合成。
Adv Enzymol Relat Areas Mol Biol. 1971;35:35-77. doi: 10.1002/9780470122808.ch2.
6
The biosynthesis of folic acid compounds in plants. 3. Distribution of the dihydropteroate-synthesizing enzyme in plants.
J Vitaminol (Kyoto). 1970 Sep;16(3):196-200. doi: 10.5925/jnsv1954.16.196.
7
The biosynthesis of folic acid compounds in plants. IV. Purification and properties of the dihydropteroate-synthesizing enzyme from pea seedlings.植物中叶酸化合物的生物合成。IV. 豌豆幼苗二氢蝶酸合成酶的纯化及性质
J Vitaminol (Kyoto). 1970 Sep;16(3):201-9. doi: 10.5925/jnsv1954.16.201.
8
[Biosynthesis of folic acid and biopterin (author's transl)].
Tanpakushitsu Kakusan Koso. 1975 Jun;20(7):691-9.
9
Enzymatic synthesis of the pteridine moiety of dihydrofolate from guanine nucleotides.
J Biol Chem. 1965 Nov;240(11):4449-53.
10
The formation of rhizopterin and formylated folate polyglutamates during the growth of Staphylococcus epidermidis.
Can J Microbiol. 1972 Jun;18(6):833-9. doi: 10.1139/m72-129.

引用本文的文献

1
Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes.青霉素与细菌细胞的相互作用：青霉素结合蛋白和青霉素敏感酶。
Bacteriol Rev. 1974 Sep;38(3):291-335. doi: 10.1128/br.38.3.291-335.1974.
2
7-Methylpterin and 7-methyllumizine: oxidative degradation products of 7-methyl-substituted pteridines in methanogenic bacteria.7-甲基蝶呤和7-甲基鲁米嗪：产甲烷菌中7-甲基取代蝶啶的氧化降解产物。
J Bacteriol. 1985 May;162(2):516-20. doi: 10.1128/jb.162.2.516-520.1985.
3
Biosynthesis of the 7-methylated pterin of methanopterin.
甲烷蝶呤7-甲基化蝶呤的生物合成。
J Bacteriol. 1986 Jan;165(1):215-8. doi: 10.1128/jb.165.1.215-218.1986.
4
Sulfonamide resistance in Streptococcus pneumoniae: DNA sequence of the gene encoding dihydropteroate synthase and characterization of the enzyme.肺炎链球菌中的磺胺耐药性：编码二氢蝶酸合酶的基因的DNA序列及该酶的特性
J Bacteriol. 1987 Sep;169(9):4320-6. doi: 10.1128/jb.169.9.4320-4326.1987.
5
An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required for synthesis of para-aminobenzoic acid, and the dihydropteroate synthase gene.一个明显的枯草芽孢杆菌叶酸生物合成操纵子，包含对氨基苯甲酸合成基因、一个兼性的色氨酸合成酶基因、对氨基苯甲酸合成所需的第三个基因以及二氢蝶酸合酶基因。
J Bacteriol. 1990 Dec;172(12):7211-26. doi: 10.1128/jb.172.12.7211-7226.1990.
6
Purification and partial characterization of 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase and 7,8-dihydropteroate synthase from Escherichia coli MC4100.来自大肠杆菌MC4100的7,8-二氢-6-羟甲基蝶呤-焦磷酸激酶和7,8-二氢蝶酸合酶的纯化及部分特性分析
J Bacteriol. 1991 Nov;173(21):7029-32. doi: 10.1128/jb.173.21.7029-7032.1991.
7
Cloning, sequence analysis, and overexpression of Escherichia coli folK, the gene coding for 7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase.大肠杆菌folK基因（编码7,8-二氢-6-羟甲基蝶呤-焦磷酸激酶）的克隆、序列分析及过表达
J Bacteriol. 1992 Sep;174(18):5971-7. doi: 10.1128/jb.174.18.5971-5977.1992.
8
Sulfonamide resistance mechanism in Escherichia coli: R plasmids can determine sulfonamide-resistant dihydropteroate synthases.大肠杆菌中的磺胺耐药机制：R质粒可决定对磺胺耐药的二氢蝶酸合酶。
Proc Natl Acad Sci U S A. 1975 Jul;72(7):2621-5. doi: 10.1073/pnas.72.7.2621.