Activity difference between α-COOH and β-COOH in N-phosphorylaspartic acids

被引:31
作者
Chen, ZZ
Tan, B
Li, YM [1 ]
Zhao, YF
Tong, YF
Wang, JF
机构
[1] Tsinghua Univ, Dept Chem, Key Lab Bioorgan Phosphorus Chem, Educ Minist, Beijing 100084, Peoples R China
[2] Acad Sinica, Natl Lab Biomacromol, Inst Biophys, Ctr Mol Biol, Beijing 100101, Peoples R China
关键词
D O I
10.1021/jo0300082
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
N-phosphorylamino acids are chemically active species that have many biomimic activities. alpha-COOH in amino acids and peptides behaviors rather differently than beta-COOH in many biochemical processes and takes a more important role in the origin of life. Activity differences between alpha-COOH and beta-COOH in the peptide formation of phosphoryl amino acids are studied by 1D, 2D NMR techniques and by ab initio and density functional theory (DFT) calculations in this paper. Phosphoryl dipeptide is formed directly from phosphoryl aspartic acids without any coupling reagents. Only the alpha-dipeptide ester is observed by 1D H-1, C-13, and P-31? NMR and 2D NMR. In the ab initio and DFT calculations, the pentacoordinate phosphorane intermediates containing five-membered rings are predicted to be more favored than those with six-membered rings. Both the experimental results and the theoretical calculations suggest that only the alpha-COOH group is activated by N-phosphorylation in N-phosphorylaspartic acid under mild conditions.
引用
收藏
页码:4052 / 4058
页数:7
相关论文
共 44 条
[1]   SENSITIVITY-ENHANCED TWO-DIMENSIONAL HETERONUCLEAR SHIFT CORRELATION NMR-SPECTROSCOPY [J].
BAX, A ;
SUBRAMANIAN, S .
JOURNAL OF MAGNETIC RESONANCE, 1986, 67 (03) :565-569
[2]   DENSITY-FUNCTIONAL THERMOCHEMISTRY .3. THE ROLE OF EXACT EXCHANGE [J].
BECKE, AD .
JOURNAL OF CHEMICAL PHYSICS, 1993, 98 (07) :5648-5652
[3]   Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation [J].
Bernstein, BE ;
Michels, PAM ;
Hol, WGJ .
NATURE, 1997, 385 (6613) :275-278
[4]   SEQUENTIAL RESONANCE ASSIGNMENTS IN PROTEIN H-1 NUCLEAR MAGNETIC-RESONANCE SPECTRA - COMPUTATION OF STERICALLY ALLOWED PROTON PROTON DISTANCES AND STATISTICAL-ANALYSIS OF PROTON PROTON DISTANCES IN SINGLE-CRYSTAL PROTEIN CONFORMATIONS [J].
BILLETER, M ;
BRAUN, W ;
WUTHRICH, K .
JOURNAL OF MOLECULAR BIOLOGY, 1982, 155 (03) :321-346
[5]   IDENTIFICATION OF AN ISOASPARTYL LINKAGE FORMED UPON DEAMIDATION OF BOVINE CALBINDIN-D9K AND STRUCTURAL CHARACTERIZATION BY 2D H-1-NMR [J].
CHAZIN, WJ ;
KORDEL, J ;
THULIN, E ;
HOFMANN, T ;
DRAKENBERG, T ;
FORSEN, S .
BIOCHEMISTRY, 1989, 28 (21) :8646-8653
[6]  
Chen ZZ, 2001, INT J QUANTUM CHEM, V83, P41, DOI 10.1002/qua.1041
[7]  
CORBRIDGE DEC, 1995, PHOSOHOROUS OUTLINE, pCH13
[8]  
EMSLEY J, 1976, CHEM PHOSPHORUS, pCH2
[9]  
Frisch M.J., 1998, GAUSSIAN98 REVISION
[10]  
Frisch M.J., 2016, Gaussian 16 Revision C. 01. 2016, V16, P01