Crystal structure of the catalytic domain of PigE: A transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp FS14
文献类型：期刊论文
| 作者 | Lou, XD ; Ran, TT ; Han, N ; Gao, YY ; He, JH ; Tang, L ; Xu, DQ ; Wang, WW |
| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2014 |
| 卷号 | 447期号:1页码:178—183 |
| 关键词 | GENE-CLUSTER PRODIGIOSIN AMINOTRANSFERASE ENZYME STREPTOMYCES COMPLEXES PATHWAY ALPHA |
| ISSN号 | 0006-291X |
| 通讯作者 | dqxu@njau.edu.cn ; wwwang@njau.edu.cn |
| 英文摘要 | Prodigiosin, a tripyrrole red pigment synthesized by Serratia and some other microbes through a bifurcated biosynthesis pathway, MBC (4-methoxy-2,2'-bipyrrole-5-carbaldehyde) and MAP (2-methyl-3-n-amyl-pyrrole) are synthesized separately and then condensed by PigC to form prodigiosin. MAP is synthesized sequentially by PigD, PigE and PigB. PigE catalyzes the transamination of an amino group to the aldehyde group of 3-acetyloctanal, resulting in an aminoketone, which spontaneously cyclizes to form H(2)MAP. Here we report the crystal structure of the catalytic domain of PigE which involved in the biosynthesis of prodigiosin precursor MAP for the first time to a resolution of 2.3 angstrom with a homodimer in the asymmetric unit. The monomer of PigE catalytic domain is composed of three domains with PLP as cofactor: a small N-terminal domain connecting the catalytic domain with the front part of PigE, a large PLP-binding domain and a C-terminal domain. The residues from both monomers build the PLP binding site at the interface of the dimer which resembles the other PLP-dependent enzymes. Structural comparison of PigE with Thermus thermophilus AcOAT showed a higher hydrophobic and smaller active site of PigE, these differences may be the reason for substrate specificity. (C) 2014 Elsevier Inc. All rights reserved. |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000335806700029 |
| 公开日期 | 2015-03-13 |
| 源URL | [http://ir.sinap.ac.cn/handle/331007/14063]  |
| 专题 | 上海应用物理研究所_中科院上海应用物理研究所2011-2017年 |
| 推荐引用方式 GB/T 7714 | Lou, XD,Ran, TT,Han, N,et al. Crystal structure of the catalytic domain of PigE: A transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp FS14[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2014,447(1):178—183. |
| APA | Lou, XD.,Ran, TT.,Han, N.,Gao, YY.,He, JH.,...&Wang, WW.(2014).Crystal structure of the catalytic domain of PigE: A transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp FS14.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,447(1),178—183. |
| MLA | Lou, XD,et al."Crystal structure of the catalytic domain of PigE: A transaminase involved in the biosynthesis of 2-methyl-3-n-amyl-pyrrole (MAP) from Serratia sp FS14".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 447.1(2014):178—183. |
入库方式： OAI收割
来源：上海应用物理研究所
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