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1
Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli.氨甲酰磷酸：大肠杆菌天冬氨酸转氨甲酰酶的别构底物
Proc Natl Acad Sci U S A. 1968 Aug;60(4):1442-9. doi: 10.1073/pnas.60.4.1442.
2
Conformational changes in aspartate transcarbamylase. IV. Ligand effects on intersubunit interactions.天冬氨酸转氨甲酰酶的构象变化。IV. 配体对亚基间相互作用的影响。
J Biol Chem. 1972 Jun 25;247(12):3829-37.
3
Relaxation spectra of aspartate transcarbamylase. Interaction of the catalytic subunit with carbamyl phosphate, succinate, and L-malate.天冬氨酸转氨甲酰酶的弛豫光谱。催化亚基与氨甲酰磷酸、琥珀酸和L-苹果酸的相互作用。
Biochemistry. 1971 Mar 16;10(6):1046-50. doi: 10.1021/bi00782a017.
4
Aspartate transcarbamylase. Kinetic studies of the catalytic subunit.天冬氨酸转氨甲酰酶。催化亚基的动力学研究。
J Biol Chem. 1969 Apr 10;244(7):1846-59.
5
A model for nucleotide regulation of aspartate transcarbamylase.天冬氨酸转氨甲酰酶的核苷酸调节模型。
Biochemistry. 1972 Aug 1;11(16):3136-42. doi: 10.1021/bi00766a029.
6
Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with carbamyl phosphate.天冬氨酸转氨甲酰酶的弛豫光谱。天然酶与氨甲酰磷酸的相互作用。
Biochemistry. 1971 May 25;10(11):2150-6. doi: 10.1021/bi00787a030.
7
Reaction of the catalytic subunit of Escherichia coli aspartate transcarbamylase with permanganate ion, a reactive structural analogue of phosphate ion.
J Biol Chem. 1971 May 25;246(10):3151-9.
8
Mechanism of the reaction catalyzed by the catalytic subunit of aspartate transcarbamylase. Kinetic studies with carbamyl phosphate as substrate.天冬氨酸转氨甲酰酶催化亚基所催化反应的机制。以氨甲酰磷酸为底物的动力学研究。
Biochemistry. 1973 Nov 6;12(23):4718-26. doi: 10.1021/bi00747a600.
9
Aspartate transcarbamylase. Stereospecific restrictions on the binding site for L-aspartate.天冬氨酸转氨甲酰酶。对L-天冬氨酸结合位点的立体特异性限制。
J Biol Chem. 1970 Mar 10;245(5):1175-9.
10
Aspartate transcarbamylase. Studies of the catalytic subunit by ultraviolet difference spectroscopy.天冬氨酸转氨甲酰酶。通过紫外差示光谱法对催化亚基的研究。
J Biol Chem. 1969 Apr 10;244(7):1869-77.

引用本文的文献

1
Replacement of Asp-162 by Ala prevents the cooperative transition by the substrates while enhancing the effect of the allosteric activator ATP on E. coli aspartate transcarbamoylase.将天冬氨酸-162替换为丙氨酸可阻止底物的协同转变，同时增强变构激活剂ATP对大肠杆菌天冬氨酸转氨甲酰酶的作用。
Protein Sci. 2002 May;11(5):1074-81. doi: 10.1110/ps.4500102.
2
Allosteric regulation of catalytic activity: Escherichia coli aspartate transcarbamoylase versus yeast chorismate mutase.催化活性的变构调节：大肠杆菌天冬氨酸转氨甲酰酶与酵母分支酸变位酶的比较
Microbiol Mol Biol Rev. 2001 Sep;65(3):404-21, table of contents. doi: 10.1128/MMBR.65.3.404-421.2001.
3
Conversion of the allosteric regulatory patterns of aspartate transcarbamoylase by exchange of a single beta-strand between diverged regulatory chains.通过在分化的调节链之间交换单个β链来改变天冬氨酸转氨甲酰酶的变构调节模式。
Biochemistry. 1997 Mar 18;36(11):3126-32. doi: 10.1021/bi962065d.
4
Peptide-protein interaction markedly alters the functional properties of the catalytic subunit of aspartate transcarbamoylase.肽与蛋白质的相互作用显著改变了天冬氨酸转氨甲酰酶催化亚基的功能特性。
Protein Sci. 1993 Jan;2(1):103-12. doi: 10.1002/pro.5560020111.
5
Molecular dynamics simulations and rigid body (TLS) analysis of aspartate carbamoyltransferase: evidence for an uncoupled R state.天冬氨酸氨甲酰基转移酶的分子动力学模拟与刚体（TLS）分析：非偶联R态的证据
Protein Sci. 1993 Jun;2(6):927-35. doi: 10.1002/pro.5560020606.
6
A 70-amino acid zinc-binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer.来自天冬氨酸转氨甲酰酶调节链的一个70个氨基酸的锌结合多肽片段导致催化三聚体的动力学机制发生显著变化。
Protein Sci. 1994 Jun;3(6):967-74. doi: 10.1002/pro.5560030612.
7
Metal cation influence on activity and regulation of aspartate carbamoyltransferase.金属阳离子对天冬氨酸氨甲酰基转移酶活性及调节的影响。
Proc Natl Acad Sci U S A. 1981 Feb;78(2):898-902. doi: 10.1073/pnas.78.2.898.
8
Isolation and preliminary characterization of single amino acid substitution mutants of aspartate carbamoyltransferase.天冬氨酸氨甲酰基转移酶单氨基酸取代突变体的分离及初步鉴定
Proc Natl Acad Sci U S A. 1980 Jun;77(6):3249-53. doi: 10.1073/pnas.77.6.3249.
9
Gross quaternary changes in aspartate carbamoyltransferase are induced by the binding of N-(phosphonacetyl)-L-aspartate: A 3.5-A resolution study.N-（膦酰乙酰基）-L-天冬氨酸的结合诱导了天冬氨酸氨甲酰基转移酶的四级结构显著变化：一项3.5埃分辨率的研究。
Proc Natl Acad Sci U S A. 1982 May;79(10):3125-8. doi: 10.1073/pnas.79.10.3125.
10
Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution.大肠杆菌未结合天冬氨酸氨甲酰基转移酶在2.6埃分辨率下的结构
Proc Natl Acad Sci U S A. 1984 Jul;81(13):4037-40. doi: 10.1073/pnas.81.13.4037.

本文引用的文献

1
ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL.关于别构转变的本质：一个合理的模型。
J Mol Biol. 1965 May;12:88-118. doi: 10.1016/s0022-2836(65)80285-6.
2
KINETICS OF REGULATORY ENZYMES. KINETIC ORDER OF THE YEAST DIPHOSPHOPYRIDINE NUCLEOTIDE ISOCITRATE DEHYDROGENASE REACTION AND A MODEL FOR THE REACTION.调节酶的动力学。酵母二磷酸吡啶核苷酸异柠檬酸脱氢酶反应的动力学级数及反应模型。
J Biol Chem. 1965 Jun;240:2682-90.
3
DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.圆盘电泳。II. 方法及其在人血清蛋白中的应用。
Ann N Y Acad Sci. 1964 Dec 28;121:404-27. doi: 10.1111/j.1749-6632.1964.tb14213.x.
4
ASPARTATE TRANSCARBAMYLASE, AN ENZYME DESIGNED FOR FEEDBACK INHIBITION.天冬氨酸转氨甲酰酶，一种为反馈抑制而设计的酶。
Fed Proc. 1964 May-Jun;23:727-35.
5
END-PRODUCT INHIBITION OF ASPARTATE TRANSCARBAMYLASE IN VARIOUS SPECIES.不同物种中天冬氨酸转氨甲酰酶的终产物抑制作用
Arch Biochem Biophys. 1964 Mar;104:438-47. doi: 10.1016/0003-9861(64)90487-4.
6
The enzymology of control by feedback inhibition.反馈抑制控制的酶学
J Biol Chem. 1962 Mar;237:891-6.
7
Control of pyrimidine biosynthesis in Escherichia coli by a feed-back mechanism.大肠杆菌中嘧啶生物合成的反馈调节机制。
J Biol Chem. 1956 Aug;221(2):757-70.
8
Studies on the biosynthesis of carbamylaspartic acid.氨甲酰天冬氨酸生物合成的研究。
J Biol Chem. 1956 May;220(1):57-70.
9
Measurement of cell growth in tissue culture with a phenol reagent (folin-ciocalteau).用酚试剂（福林-西奥卡泰奥试剂）测量组织培养中的细胞生长
Proc Soc Exp Biol Med. 1956 Feb;91(2):305-7. doi: 10.3181/00379727-91-22245.
10
Substrate- and inhibitor-induced changes in the optical rotatory dispersion of aspartate transcarbamylase.底物和抑制剂诱导的天冬氨酸转氨甲酰酶旋光色散变化。
Nature. 1966 Jul 30;211(5048):497-501. doi: 10.1038/211497a0.

Carbamyl phosphate: an allosteric substrate for aspartate transcarbamylase of Escherichia coli.

作者信息

Bethell M R, Smith K E, White J S, Jones M E

出版信息

Proc Natl Acad Sci U S A. 1968 Aug;60(4):1442-9. doi: 10.1073/pnas.60.4.1442.

DOI:10.1073/pnas.60.4.1442
PMID:4877273
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC224939/
Abstract
摘要