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D-4-脱氧-5-氧代葡萄糖酸水解酶(脱羧)的纯化及性质

Purification and properties of D-4-deoxy-5-oxoglucarate hydro-lyase (decarboxylating).

作者信息

Jeffcoat R, Hassall H, Dagley S

出版信息

Biochem J. 1969 Dec;115(5):977-83. doi: 10.1042/bj1150977.

DOI:10.1042/bj1150977
PMID:4982840
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1185240/
Abstract
  1. An enzyme extracted from Pseudomonas acidovorans was purified and shown to catalyse the simultaneous dehydration and decarboxylation of d-4-deoxy-5-oxoglucarate. It is proposed to name the enzyme d-4-deoxy-5-oxoglucarate hydro-lyase (decarboxylating), trivial name ;deoxyoxoglucarate dehydratase'. 2. No added cofactors were required, and the enzyme was inactivated when incubated with its substrate in the presence of sodium borohydride. Under these conditions the substrate and enzyme appeared to be bound covalently. 3. The action of the enzyme is readily explained if it is assumed that d-4-deoxy-5-oxoglucarate forms a Schiff base with a lysine residue in the enzyme.
摘要
  1. 从食酸假单胞菌中提取的一种酶被纯化,并显示其能催化d-4-脱氧-5-氧代葡萄糖酸的同时脱水和脱羧反应。建议将该酶命名为d-4-脱氧-5-氧代葡萄糖酸水解酶(脱羧),俗名“脱氧氧代葡萄糖酸脱水酶”。2. 不需要添加辅因子,当在硼氢化钠存在下与底物一起孵育时,该酶会失活。在这些条件下,底物和酶似乎以共价键结合。3. 如果假设d-4-脱氧-5-氧代葡萄糖酸与酶中的赖氨酸残基形成席夫碱,那么该酶的作用很容易解释。
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e819/1185240/d2c1f5840de5/biochemj00688-0125-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e819/1185240/d2c1f5840de5/biochemj00688-0125-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e819/1185240/d2c1f5840de5/biochemj00688-0125-a.jpg

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