3ALPHA-羟基类固醇脱氢酶 | 9028-56-2

• 物质功能分类: 食品添加剂 - 酶制剂
• 分子结构分类: 氧化还原酶 - 作用于CH-OH供体组 - 以NAD+或NADP+为受体
• 中文名称: 3ALPHA-羟基类固醇脱氢酶
• 中文别名: 3α-羟基类固醇脱氢酶；乳酸脱氢酶；3-α羟基类固醇脱氢酶
• 英文名称: 3alpha-hydroxysteroid 3-dehydrogenase (Si-specific)
• 英文别名: hydroxyprostaglandin dehydrogenase；3alpha-hydroxysteroid oxidoreductase；sterognost 3alpha；3alpha-hydroxysteroid dehydrogenase (B-specific)；3alpha-hydroxysteroid 3-dehydrogenase (B-specific)；3alpha-hydroxysteroid:NAD(P)+ 3-oxidoreductase (B-specific)；15-hydroxyprostaglandin dehydrogenase
• CAS: 9028-56-2

安全信息

• 安全说明：
  S24/25
• WGK Germany：
  3
• 海关编码：
  35079090

制备方法与用途

简介

3α-羟类固醇脱氢酶是一种由睾酮丛毛单胞菌分泌的类固醇脱氢酶，含有258个氨基酸残基，理论分子量为26.4kD。该酶可逆地催化C19-27类固醇3位羟基/酮基的氧化还原反应，作用于多种类固醇基质。其等电点为4.8，最适pH值在7-9之间。汞离子（Hg²⁺）、银离子（Ag⁺）等会抑制酶活性，而金属离子螯合剂如EDTA不会抑制酶活，并且能在一定程度上对酶的稳定和保存提供帮助。

应用

3α-羟基类固醇脱氢酶为白色微黄无定形粉末。胆汁酸是其一种作用底物，在临床上通过催化羟基类固醇的脱氢反应来检测总胆汁酸含量，具有重要的临床应用价值。

反应信息

• 作为试剂：
  描述：

  地诺前列酮 在 3ALPHA-羟基类固醇脱氢酶 盐酸 、 nicotinamide adenine dinucleotide 、 三羟甲基氨基甲烷 作用下， 以 水 为溶剂， 生成 (5Z,11alpha,13E)-11-羟基-9,15-二氧代-前列腺-5,13-二烯-1-酸
  参考文献：
  名称：

  Role of glutamine 148 of human 15-hydroxyprostaglandin dehydrogenase in catalytic oxidation of prostaglandin E2

  摘要：

  NAD(+)-dependent 15-hydroxyprostaglandin dehydrogenase (15-PGDH), a member of the short-chain dehydrogenase/reductase (SDR) family, catalyzes the first step in the catabolic pathways of prostaglandins and lipoxins. This enzyme oxidizes the C-15 hydroxyl group of prostaglandins and lipoxins to produce 15-keto metabolites which exhibit greatly reduced biological activities. A three-dimensional (3D) structure of 15-PGDH based on the crystal structures of the levodione reductase and tropinone reductase-II was generated and used for docking study with NAD(+) coenzyme and PGE(2) substrate. Three well-conserved residues among SDR family which correspond to Ser-138, Tyr-151, and Lys-155 of 15-PGDH have been shown to participate in the catalytic reaction. Based on the molecular interactions observed from 3D structure of 15-PGDH, we further propose that Gln-148 in 15-PGDH is important in properly positioning the 15-hydroxyl group of PGE(2) by hydrogen bonding with the side-chain oxygen atom of Gln-148. This residue is found to be less conserved and replaceable by glutamyl, histidinyl, and asparaginyl residues in SDR family. Accordingly, site-directed mutagenesis of Gln-148 of 15-PGDH to alanine, glutamic acid, histidine, and asparagine (Q148A, Q148E, Q148H, and Q148N) was carried out. The activity of mutant Q148A was not detectable, whereas those of mutants Q148E, Q148H, and Q148N were comparable to or higher than the wild type. This indicates that the side-chain oxygen or nitrogen atom at position 148 of 15-PGDH plays an important role in anchoring C-15 hydroxyl group of PGE2 through hydrogen bonding for catalytic reaction. (c) 2006 Elsevier Ltd. All rights reserved.

  DOI：

  10.1016/j.bmc.2006.06.030