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2
Overexpression of prolylcarboxypeptidase enhances plasma prekallikrein activation on Chinese hamster ovary cells.脯氨酰羧肽酶的过表达增强了中国仓鼠卵巢细胞上血浆前激肽释放酶的激活。
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Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families.
J Biol Chem. 1993 Aug 5;268(22):16631-8.
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Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.S28蛋白酶家族的结构定义与底物特异性：人脯氨酰羧肽酶的晶体结构
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A digestive prolyl carboxypeptidase in Tenebrio molitor larvae.黄粉虫幼虫中的一种消化脯氨酰羧肽酶。
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Crystallization of serine carboxypeptidases.丝氨酸羧肽酶的结晶
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9
Characterisation and preliminary X-ray diffraction analysis of human pancreatic procarboxypeptidase A2.人胰腺羧肽酶原A2的表征及初步X射线衍射分析
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Prolylcarboxypeptidase deficiency is associated with increased blood pressure, glomerular lesions, and cardiac dysfunction independent of altered circulating and cardiac angiotensin II.脯氨酰羧肽酶缺乏与血压升高、肾小球病变及心脏功能障碍相关，且与循环及心脏中的血管紧张素II改变无关。
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Prolyl carboxypeptidase mRNA expression in the mouse brain.脯氨酰羧肽酶 mRNA 在小鼠脑中的表达。
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2
Ghrelin regulates hypothalamic prolyl carboxypeptidase expression in mice.生长激素释放肽调节小鼠下丘脑脯氨酰羧肽酶的表达。
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3
Prolyl carboxypeptidase and its inhibitors in metabolism.脯氨酰羧肽酶及其抑制剂在代谢中的作用。
Trends Endocrinol Metab. 2013 Feb;24(2):61-7. doi: 10.1016/j.tem.2012.11.001. Epub 2012 Dec 12.
4
Murine prolylcarboxypeptidase depletion induces vascular dysfunction with hypertension and faster arterial thrombosis.鼠脯氨酰羧肽酶耗竭诱导血管功能障碍伴高血压和更快的动脉血栓形成。
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5
Structural definition and substrate specificity of the S28 protease family: the crystal structure of human prolylcarboxypeptidase.S28蛋白酶家族的结构定义与底物特异性：人脯氨酰羧肽酶的晶体结构
BMC Struct Biol. 2010 Jun 11;10:16. doi: 10.1186/1472-6807-10-16.

本文引用的文献

1
Processing of X-ray diffraction data collected in oscillation mode.振荡模式下收集的X射线衍射数据的处理。
Methods Enzymol. 1997;276:307-26. doi: 10.1016/S0076-6879(97)76066-X.
2
Structural basis of human p70 ribosomal S6 kinase-1 regulation by activation loop phosphorylation.人源 p70 核糖体 S6 激酶-1 通过激活环磷酸化调节的结构基础。
J Biol Chem. 2010 Feb 12;285(7):4587-94. doi: 10.1074/jbc.M109.040667. Epub 2009 Oct 28.
3
Prolylcarboxypeptidase regulates food intake by inactivating alpha-MSH in rodents.脯氨酰羧肽酶通过使啮齿动物体内的α-促黑素失活来调节食物摄入。
J Clin Invest. 2009 Aug;119(8):2291-303. doi: 10.1172/JCI37209. Epub 2009 Jul 20.
4
Prolylcarboxypeptidase: a cardioprotective enzyme.脯氨酰羧肽酶：一种具有心脏保护作用的酶。
Int J Biochem Cell Biol. 2009 Mar;41(3):477-81. doi: 10.1016/j.biocel.2008.02.022. Epub 2008 Feb 29.
5
Recombinant prolylcarboxypeptidase activates plasma prekallikrein.重组脯氨酰羧肽酶激活血浆前激肽释放酶。
Blood. 2004 Jun 15;103(12):4554-61. doi: 10.1182/blood-2003-07-2510. Epub 2004 Mar 2.
6
Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator.脯氨酰羧肽酶作为内皮细胞前激肽释放酶激活剂的鉴定与特性分析。
J Biol Chem. 2002 May 17;277(20):17962-9. doi: 10.1074/jbc.M106101200. Epub 2002 Feb 5.
7
Sequencing and cloning of human prolylcarboxypeptidase (angiotensinase C). Similarity to both serine carboxypeptidase and prolylendopeptidase families.
J Biol Chem. 1993 Aug 5;268(22):16631-8.
8
Solvent content of protein crystals.蛋白质晶体的溶剂含量。
J Mol Biol. 1968 Apr 28;33(2):491-7. doi: 10.1016/0022-2836(68)90205-2.
9
Purification and properties of prolylcarboxypeptidase (angiotensinase C) from human kidney.人肾脯氨酰羧肽酶（血管紧张素酶C）的纯化及性质
J Biol Chem. 1978 Sep 10;253(17):5927-31.

人脯氨酰羧肽酶的表达、纯化及结晶

Expression, purification and crystallization of human prolylcarboxypeptidase.

作者信息

Abeywickrema Pravien D, Patel Sangita B, Byrne Noel J, Diehl Ronald E, Hall Dawn L, Ford Rachael E, Rickert Keith W, Reid John C, Shipman Jennifer M, Geissler Wayne M, Pryor Kelly D, SinhaRoy Ranabir, Soisson Stephen M, Lumb Kevin J, Sharma Sujata

机构信息

Global Structural Biology, Merck Research Laboratories, West Point, PA 19486, USA.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt 6):702-5. doi: 10.1107/S1744309110014041. Epub 2010 May 27.

DOI:10.1107/S1744309110014041
PMID:20516604
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2882774/
Abstract

Prolylcarboxypeptidase (PrCP) is a lysosomal serine carboxypeptidase that cleaves a variety of C-terminal amino acids adjacent to proline and has been implicated in diseases such as hypertension and obesity. Here, the robust production, purification and crystallization of glycosylated human PrCP from stably transformed CHO cells is described. Purified PrCP yielded crystals belonging to space group R32, with unit-cell parameters a = b = 181.14, c = 240.13 A, that diffracted to better than 2.8 A resolution.

摘要

脯氨酰羧肽酶（PrCP）是一种溶酶体丝氨酸羧肽酶，可切割脯氨酸附近的多种C端氨基酸，并与高血压和肥胖等疾病有关。本文描述了从稳定转化的CHO细胞中大量生产、纯化和结晶糖基化人PrCP的过程。纯化后的PrCP产生了属于空间群R32的晶体，晶胞参数a = b = 181.14，c = 240.13 Å，其衍射分辨率优于2.8 Å。