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酿酒酵母中L-天冬酰胺酶I与天冬酰胺酶II之间的遗传和生理关系。

Genetic and physiological relationships between L-asparaginase I and asparaginase II in Saccharomyces cerevisiae.

作者信息

Jones G E

出版信息

J Bacteriol. 1977 Apr;130(1):128-30. doi: 10.1128/jb.130.1.128-130.1977.

Abstract

The cistron that codes for L-asparaginase I in Saccharomyces cerevisiae (aspl) is not genetically linked to either of the cistrons coding for expression of asparaginase II (asp2 and asp3). Cells containing different combinations of theses enzymes grow at different rates in media in which L-asparagine or D-asparagine is the only source of nitrogen for cell replication. Cells lacking L-asparaginase I but possessing asparaginase II grow more rapidly in medium containing D-asparagine as a nitrogen source than cells containing both enzymes, even though D-asparagine is not a substrate of L-asparaginase I. These results indicate that L-asparaginase I and asparaginase II interact in some way to regulate the utilization of asparagine as a nitrogen source for cell growth.

摘要

酿酒酵母中编码L-天冬酰胺酶I(aspl)的顺反子与编码天冬酰胺酶II(asp2和asp3)表达的任何一个顺反子都没有遗传联系。含有这些酶不同组合的细胞,在以L-天冬酰胺或D-天冬酰胺作为细胞复制唯一氮源的培养基中,生长速率不同。缺乏L-天冬酰胺酶I但拥有天冬酰胺酶II的细胞,在以D-天冬酰胺作为氮源的培养基中,比同时含有这两种酶的细胞生长得更快,尽管D-天冬酰胺不是L-天冬酰胺酶I的底物。这些结果表明,L-天冬酰胺酶I和天冬酰胺酶II以某种方式相互作用,以调节天冬酰胺作为细胞生长氮源的利用。

相似文献

2
Utilization of D-asparagine by Saccharomyces cerevisiae.酿酒酵母对D-天冬酰胺的利用
J Bacteriol. 1976 Mar;125(3):999-1004. doi: 10.1128/jb.125.3.999-1004.1976.

本文引用的文献

1
L-asparaginase-deficient mutants of yeast.
Science. 1970 Jan 9;167(3915):181-2. doi: 10.1126/science.167.3915.181.
3
L-asparaginase: a review.L-天冬酰胺酶综述
Adv Enzymol Relat Areas Mol Biol. 1973;39:185-248. doi: 10.1002/9780470122846.ch3.
4
Biochemical properties of yeast L-asparaginase.酵母L-天冬酰胺酶的生化特性
Biochem Genet. 1973 Jun;9(2):131-46. doi: 10.1007/BF00487443.
5
A fine-structure map of the yeast l-asparaginase gene.
Mol Gen Genet. 1973;121(1):9-14. doi: 10.1007/BF00353689.
6
Utilization of D-asparagine by Saccharomyces cerevisiae.酿酒酵母对D-天冬酰胺的利用
J Bacteriol. 1976 Mar;125(3):999-1004. doi: 10.1128/jb.125.3.999-1004.1976.

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