2篇
您的检索式：作者名="Prajwalini Mehere"
|
|
|
题名
|
作者
|
年代
|
出处
|
被引量
|
| 1 | Tyrosine metabolic enzymes from insects and mammals:A comparative perspective显示文摘在在昆虫和哺乳动物之间的酷氨酸的新陈代谢的差别举分子的进化的一个有趣的例子。昆虫和哺乳动物拥有酶的调整系统为酷氨酸代谢物遇见他们的特定的要求;然而,涉及酷氨酸新陈代谢的更相应的酶出现在许多昆虫种类。没有现代 genomics 的知识,一个人可能假定哺乳动物,通常比昆虫更复杂并且为重要 catecholamine neurotransmitters 并且为黑素作为一位先锋要求酷氨酸,应该拥有更多的酶控制酷氨酸新陈代谢。因此,昆虫为什么实际上拥有更多的酷氨酸的问题新陈代谢的酶相当有趣。昆虫为表皮变硬并且为天生的有免疫力的回答重重地依靠酷氨酸新陈代谢,这长被知道了,并且这些进化限制是可能的这个问题的关键答案。以 melanogenesis,哺乳动物也拥有规定的高水平;而昆虫加速象 melanogenesis 一样的小径必须因此忍受增加的氧化压力,然而哺乳动物的系统为 detoxification 拥有更多的机制。我们的研究组有机会描绘从昆虫和哺乳动物涉及酷氨酸新陈代谢的许多关键蛋白质的结构和功能。在这微型评论,我们将与昆虫相比在哺乳动物的一个进化观点的范围给我们关于酷氨酸的研究的简短概述新陈代谢的酶。 | Christopher John Vavricka Qian Han Prajwalini Mehere Haizhen Ding Bruce M. Christensen and Jianyong Li | 2014 | Insect Science2014，21，1： | 4 |
| 2 | Tyrosine aminotransferase: biochemical and structural properties and molecular dynamics simulations显示文摘Tyrosine aminotransferase(TAT)catalyzes the transamination of tyrosine and other aromatic amino acids.The enzyme is thought to play a role in tyrosinemia type II,hepatitis and hepatic carcinoma recovery.The objective of this study is to investigate its biochemical and structural characteristics and substrate specificity in order to provide insight regarding its involvement in these diseases.Mouse TAT(mTAT)was cloned from a mouse cDNA library,and its recombinant protein was produced using Escherichia coli cells and purified using various chromatographic techniques.The recombinant mTAT is able to catalyze the transamination of tyrosine usingα-ketoglutaric acid as an amino group acceptor at neutral pH.The enzyme also can use glutamate and phenylalanine as amino group donors and p-hydroxyphenylpyruvate,phenylpyruvate and alpha-ketocaproic acid as amino group acceptors.Through macromolecular crystallography we have determined the mTAT crystal structure at 2.9Åresolution.The crystal structure revealed the interaction between the pyridoxal-5′-phosphate cofactor and the enzyme,as well as the formation of a disulphide bond.The detection of disulphide bond provides some rational explanation regarding previously observed TAT inactivation under oxidative conditions and reactivation of the inactive TAT in the presence of a reducing agent.Molecular dynamics simulations using the crystal structures of Trypanosoma cruzi TAT and human TAT provided further insight regarding the substrate-enzyme interactions and substrate specificity.The biochemical and structural properties of TAT and the binding of its cofactor and the substrate may help in elucidation of the mechanism of TAT inhibition and activation. | Prajwalini Mehere Qian Han Justin A.Lemkul Christopher J.Vavricka Howard Robinson David R.Bevan Jianyong Li | 2010 | Protein & Cell2010，1，11： | 4 |
您所在的机构暂未开通此部分的功能，请联系管理员