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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
Lou, XD; Ran, TT; Han, N; Gao, YY; He, JH; Tang, L; Xu, DQ; Wang, WW; dqxu@njau.edu.cn; wwwang@njau.edu.cn
2014
Source PublicationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN0006-291X
Volume447Issue:1Pages:178—183
AbstractProdigiosin, 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.
KeywordGene-cluster Prodigiosin Aminotransferase Enzyme Streptomyces Complexes Pathway Alpha
Indexed BySCI
Language英语
WOS IDWOS:000335806700029
Citation statistics
Cited Times:7[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.sinap.ac.cn/handle/331007/14063
Collection中科院上海应用物理研究所2011-2019年
Corresponding Authordqxu@njau.edu.cn; wwwang@njau.edu.cn
Recommended Citation
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.,...&wwwang@njau.edu.cn.(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.
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