Purification and Characterization of Monovalent Cation-Activated Levodione Reductase from Corynebacterium aquaticumM-13
Purification and Characterization of Monovalent Cation-Activated Levodione Reductase from Corynebacterium aquaticumM-13
复制标题
来自水生棒状杆菌 M-13 的单价阳离子激活左旋二酮还原酶的纯化和表征
DOI：
10.1128/aem.65.10.4399-4403.1999
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发表时间：
1999
影响因子：
4.4
通讯作者：
Sakayu Shimizu
中科院分区：
文献类型：
--
作者：
M. Wada;A. Yoshizumi;S. Nakamori;Sakayu Shimizu
摘要（6 R）-2，2，6-三甲基-1，4-环己二酮（左旋二酮）还原酶是从土壤分离物水生棒杆菌M-13的细胞提取物中分离得到的。该酶催化左旋二酮区域和立体选择性还原为（4 R，6 R）-4-羟基-2，2，6-三甲基环己酮（放线醇）。通过高效凝胶渗透色谱法和十二烷基硫酸钠-聚丙烯酰胺凝胶电泳法测得该酶的相对分子质量分别为142，000 Da和36，000 Da。该酶需要NAD+或NADH作为辅助因子，并催化放线醇和左旋二酮之间的可逆氧化还原。该酶被一价阳离子如K+、Na+和NH 4+高度活化。该酶的氨基端和部分氨基酸序列表明，它属于短链醇脱氢酶/还原酶家族。这是左旋二酮还原酶的首次报道。
ABSTRACT (6R)-2,2,6-Trimethyl-1,4-cyclohexanedione (levodione) reductase was isolated from a cell extract of the soil isolateCorynebacterium aquaticum M-13. This enzyme catalyzed regio- and stereoselective reduction of levodione to (4R,6R)-4-hydroxy-2,2,6-trimethylcyclohexanone (actinol). The relative molecular mass of the enzyme was estimated to be 142,000 Da by high-performance gel permeation chromatography and 36,000 Da by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme required NAD+ or NADH as a cofactor, and it catalyzed reversible oxidoreduction between actinol and levodione. The enzyme was highly activated by monovalent cations, such as K+, Na+, and NH4+. The NH2-terminal and partial amino acid sequences of the enzyme showed that it belongs to the short-chain alcohol dehydrogenase/reductase family. This is the first report of levodione reductase.
铜绿假单胞菌 lasA 基因的核苷酸序列和在大肠杆菌中的表达。
影响因子：
3.2
作者：
Schad,PA;Iglewski,BH
通讯作者：
Iglewski,BH