Crystal structures of fmsl and its complex with spermine reveal substrate specificity
文献类型：期刊论文
| 作者 | Huang, QQ ; Liu, Q ; Hao, Q |
| 刊名 | JOURNAL OF MOLECULAR BIOLOGY
 |
| 出版日期 | 2005 |
| 卷号 | 348期号:4页码:951 |
| 关键词 | AMINO-ACID OXIDASE SACCHAROMYCES-CEREVISIAE POLYAMINE OXIDASE ACTIVE-SITE BIOSYNTHESIS PROTEIN BINDING PROGRAM EVOLUTION HYPUSINE |
| ISSN号 | 0022-2836 |
| 通讯作者 | Hao, Q: Cornell Univ, Cornell High Energy Synchrotron Source, MacCHESS, Ithaca, NY 14853 USA. |
| 中文摘要 | Fms1 is a rate-limiting enzyme for the biosynthesis of pantothenic acid in yeast. Fms1 has polyamine oxidase (PAO) activity, which converts spermine into spermidine and 3-aminopropanal. The 3-aminopropanal is further oxidized to produce beta-alanine, which is necessary for the biosynthesis of pantothenic acid. The crystal structures of Fms1 and its complex with the substrate spermine have been determined using the single-wavelength anomalous diffraction (SAD) phasing method. Fms1 consists of an FAD-binding domain, with Rossmann fold topology, and a substrate-binding domain. The active site is a tunnel located at the interface of the two domains. The substrate spermine binds to the active site mainly via hydrogen bonds and hydrophobic interactions. In the complex, C11 but not C9 of spermine is close enough to the catalytic site (N5 of FAD) to be oxidized. Therefore, the products are spermidine and 3-aminopropanal, rather than 3-(aminopropyl) 4-aminobutyraldehyde and 1,3-diaminoprone. (c) 2005 Elsevier Ltd. All rights reserved. |
| 收录类别 | SCI |
| 语种 | 英语 |
| 公开日期 | 2013-09-17 |
| 源URL | [http://ir.iphy.ac.cn/handle/311004/35409]  |
| 专题 | 物理研究所_物理所公开发表论文_物理所公开发表论文_期刊论文 |
| 推荐引用方式 GB/T 7714 | Huang, QQ,Liu, Q,Hao, Q. Crystal structures of fmsl and its complex with spermine reveal substrate specificity[J]. JOURNAL OF MOLECULAR BIOLOGY,2005,348(4):951. |
| APA | Huang, QQ,Liu, Q,&Hao, Q.(2005).Crystal structures of fmsl and its complex with spermine reveal substrate specificity.JOURNAL OF MOLECULAR BIOLOGY,348(4),951. |
| MLA | Huang, QQ,et al."Crystal structures of fmsl and its complex with spermine reveal substrate specificity".JOURNAL OF MOLECULAR BIOLOGY 348.4(2005):951. |
入库方式： OAI收割
来源：物理研究所
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