Substrate specificity of Escherichia coli thymidine phosphorylase

被引：19
作者：
Panova, N. G.
Alexeev, C. S.
Kuzmichov, A. S.
Shcheveleva, E. V.
Gavryushov, S. A.
Polyakov, K. M.
Kritzyn, A. M.
Mikhailov, S. N.
Esipov, R. S.
Miroshnikov, A. I.
机构：
[1] Russian Acad Sci, Engelhardt Inst Mol Biol, Moscow 119991, Russia
[2] Russian Acad Sci, Shemyakin & Ovchinnikov Inst Bioorgan Chem, Moscow 117997, Russia
来源：
BIOCHEMISTRY-MOSCOW | 2007年 / 72卷 / 01期
基金：
俄罗斯基础研究基金会;
关键词：
thymidine phosphorylase; thymidine derivatives; substrate specificity; inhibitors; analysis in terms of steric interactions;
D O I：
10.1134/S0006297907010026
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Substrate specificity of Escherichia coli thymidine phosphorylase to thymidine derivatives modified at 5'-, 3'-, and 2',3'-positions of the sugar moiety was studied. Equilibrium and kinetic constants (K (m), K (I), k (cat)) of the phosphorolysis reaction have been determined for 20 thymidine analogs. The results are compared with X-ray and molecular dynamics data. The most important hydrogen bonds in the enzyme-substrate complex are revealed.
引用
收藏
页码：21 / 28
页数：8
相关论文
共 50 条
  • [31] A single amino acid substitution in aromatic hydroxylase (HpaB) of Escherichia coli alters substrate specificity of the structural isomers of hydroxyphenylacetate
    Hanseol Kim
    Sinyeon Kim
    Dohyeon Kim
    Sung Ho Yoon
    BMC Microbiology, 20
  • [32] C-terminal His-tagging results in substrate specificity changes of the thioesterase I from Escherichia coli
    Lee, YL
    Su, MS
    Huang, TH
    Shaw, JF
    JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 1999, 76 (10) : 1113 - 1118
  • [33] Analysis of in vivo substrate specificity of the PHA synthase from Ralstonia eutropha:: formation of novel copolyesters in recombinant Escherichia coli
    Antonio, RV
    Steinbüchel, A
    Rehm, BHA
    FEMS MICROBIOLOGY LETTERS, 2000, 182 (01) : 111 - 117
  • [34] Induction of thymidine phosphorylase by interferon and taxanes occurs only in human cancer cells with low thymidine phosphorylase activity
    Fukushima, M
    Okabe, H
    Takechi, T
    Ichikawa, W
    Hirayama, R
    CANCER LETTERS, 2002, 187 (1-2) : 103 - 110
  • [35] Kinetics mechanism and regulation of native human hepatic thymidine phosphorylase
    Oh, Taesung
    el Kouni, Mahmoud H.
    INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, 2019, 110 : 122 - 129
  • [36] Thymidine phosphorylase-mediated angiogenesis regulated by thymidine phosphorylase inhibitor in human ovarian cancer cells in vivo
    Tsukagoshi, S
    Saga, Y
    Suzuki, N
    Fujioka, A
    Nakagawa, F
    Fukushima, M
    Suzuki, M
    INTERNATIONAL JOURNAL OF ONCOLOGY, 2003, 22 (05) : 961 - 967
  • [37] Structural investigation of the thymidine phosphorylase from Salmonella typhimurium in the unliganded state and its complexes with thymidine and uridine
    Balaev, Vladislav V.
    Lashkov, Alexander A.
    Gabdulkhakov, Azat G.
    Dontsova, Maria V.
    Seregina, Tatiana A.
    Mironov, Alexander S.
    Betzel, Christian
    Mikhailov, Al'bert M.
    ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 2016, 72 : 224 - 233
  • [38] Accumulation of thymidine-derived sugars in thymidine phosphorylase overexpressing cells
    Bijnsdorp, I. V.
    Azijli, K.
    Jansen, E. E.
    Wamelink, M. M.
    Jakobs, C.
    Struys, E. A.
    Fukushima, M.
    Kruyt, F. A. E.
    Peters, G. J.
    BIOCHEMICAL PHARMACOLOGY, 2010, 80 (06) : 786 - 792
  • [39] Substrate specificity of the yeast protein tyrosine phosphatase, PTP1, overexpressed from an Escherichia coli expression system.
    Kwon, M
    Oh, M
    Han, J
    Cho, H
    JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, 1996, 29 (04): : 386 - 392
  • [40] Thymidine phosphorylase and dihydropyrimidine dehydrogenase in bladder cancer
    Iizumi, T
    Hariu, K
    Sato, M
    Sato, S
    Shimizu, H
    Tomomasa, H
    Umeda, T
    UROLOGIA INTERNATIONALIS, 2002, 68 (02) : 122 - 125
12345