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X-ray crystallographic and kinetic studies of oligosaccharide binding to phosphorylase.

作者信息

Kasvinsky P J, Madsen N B, Fletterick R J, Sygusch J

出版信息

J Biol Chem. 1978 Feb 25;253(4):1290-6.

PMID:624732
Abstract
摘要

相似文献

1
X-ray crystallographic and kinetic studies of oligosaccharide binding to phosphorylase.寡糖与磷酸化酶结合的X射线晶体学和动力学研究。
J Biol Chem. 1978 Feb 25;253(4):1290-6.
2
The regulation of glycogen phosphorylase alpha by nucleotide derivatives. Kinetic and x-ray crystallographic studies.核苷酸衍生物对糖原磷酸化酶α的调节作用。动力学及X射线晶体学研究。
J Biol Chem. 1978 May 10;253(9):3343-51.
3
The structures and related functions of phosphorylase a.磷酸化酶a的结构及相关功能。
Annu Rev Biochem. 1980;49:31-61. doi: 10.1146/annurev.bi.49.070180.000335.
4
The crystal structure of phosphorylase beta at 6 A resolution.
J Mol Biol. 1974 Dec 25;90(4):703-17. doi: 10.1016/0022-2836(74)90534-8.
5
Time-resolved structural studies on catalysis in the crystal with glycogen phosphorylase b.对糖原磷酸化酶b晶体中催化作用的时间分辨结构研究。
Biochem Soc Trans. 1986 Jun;14(3):538-41. doi: 10.1042/bst0140538.
6
Site-site interactions in glycogen phosphorylase b probed by ligands specific for each site.
Biochemistry. 1983 Sep 13;22(19):4460-5. doi: 10.1021/bi00288a017.
7
Allosteric transitions of phosphorylase a and the regulation of glycogen metabolism.
J Biol Chem. 1978 Dec 25;253(24):9097-101.
8
Refined crystal structure of the phosphorylase-heptulose 2-phosphate-oligosaccharide-AMP complex.磷酸化酶-庚酮糖2-磷酸-寡糖-AMP复合物的精细晶体结构
J Mol Biol. 1990 Feb 5;211(3):645-61. doi: 10.1016/0022-2836(90)90271-M.
9
Crystallographic analysis of phosphorylase alpha at 2.5 A resolution, a comment on the chemical sequence.磷酸化酶α在2.5埃分辨率下的晶体学分析：关于化学序列的注释
Biochemistry. 1978 Dec 26;17(26):5693-4.
10
Low-resolution structure of the glycogen phosphorylase alpha monomer and comparison with phosphorylase beta.
J Mol Biol. 1976 May 5;103(1):1-13. doi: 10.1016/0022-2836(76)90048-6.

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1
Kinetic and Structural Studies of the Plastidial Phosphorylase.质体磷酸化酶的动力学和结构研究
ACS Omega. 2024 Sep 25;9(40):41841-41854. doi: 10.1021/acsomega.4c06313. eCollection 2024 Oct 8.
2
A new interpretation of sulfate activation of rabbit muscle glycogen phosphorylase.兔肌糖原磷酸化酶硫酸盐激活作用的新解释。
Glycoconj J. 2018 Jun;35(3):299-309. doi: 10.1007/s10719-018-9823-x. Epub 2018 May 4.
3
Probing the catalytic site of rabbit muscle glycogen phosphorylase using a series of specifically modified maltohexaose derivatives.
使用一系列经过特殊修饰的麦芽六糖衍生物探测兔肌肉糖原磷酸化酶的催化部位。
Glycoconj J. 2017 Aug;34(4):563-574. doi: 10.1007/s10719-017-9776-5. Epub 2017 Jun 8.
4
Sensitive, nonradioactive assay of phosphorylase kinase through measurement of enhanced phosphorylase activity towards fluorogenic dextrin.通过测量对荧光糊精增强的磷酸化酶活性对磷酸化酶激酶进行灵敏的非放射性测定。
J Biochem. 2016 Feb;159(2):239-46. doi: 10.1093/jb/mvv097. Epub 2015 Sep 15.
5
The binding of beta- and gamma-cyclodextrins to glycogen phosphorylase b: kinetic and crystallographic studies.β-和γ-环糊精与糖原磷酸化酶b的结合：动力学和晶体学研究
Protein Sci. 2003 Sep;12(9):1914-24. doi: 10.1110/ps.03149503.
6
Synthesis and kinetic evaluation of 4-deoxymaltopentaose and 4-deoxymaltohexaose as inhibitors of muscle and potato alpha-glucan phosphorylases.4-脱氧麦芽五糖和4-脱氧麦芽六糖作为肌肉和马铃薯α-葡聚糖磷酸化酶抑制剂的合成及动力学评估
Biochem J. 1999 Mar 1;338 ( Pt 2)(Pt 2):251-6.
7
The crystal structure of Escherichia coli maltodextrin phosphorylase provides an explanation for the activity without control in this basic archetype of a phosphorylase.大肠杆菌麦芽糊精磷酸化酶的晶体结构为这种磷酸化酶基本原型中缺乏调控的活性提供了解释。
EMBO J. 1997 Jan 2;16(1):1-14. doi: 10.1093/emboj/16.1.1.
8
Engineered plant phosphorylase showing extraordinarily high affinity for various alpha-glucan molecules.工程化植物磷酸化酶对各种α-葡聚糖分子表现出极高的亲和力。
Protein Sci. 1993 Oct;2(10):1621-9. doi: 10.1002/pro.5560021008.
9
Potato and rabbit muscle phosphorylases: comparative studies on the structure, function and regulation of regulatory and nonregulatory enzymes.马铃薯和兔肌肉磷酸化酶：调节型和非调节型酶的结构、功能及调节的比较研究
Mol Cell Biochem. 1982 Feb 19;42(3):129-44. doi: 10.1007/BF00238507.
10
Subunit interactions and the allosteric response in phosphorylase.磷酸化酶中的亚基相互作用与别构效应
Biophys J. 1980 Oct;32(1):175-92. doi: 10.1016/S0006-3495(80)84932-0.