Newman Janet, Pearce Lesley, Lesburg Charles A, Strickland Corey, Peat Thomas S
Materials Science and Engineering, CSIRO, 343 Royal Parade, Parkville, VIC 3052, Australia.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jan 1;67(Pt 1):90-3. doi: 10.1107/S1744309110046208. Epub 2010 Dec 23.
Arginase (EC 3.5.3.1) is an aminohydrolase that acts on L-arginine to produce urea and ornithine. Two isotypes of the enzyme are found in humans. Type I is predominantly produced in the liver and is a homotrimer of 35 kDa subunits. Human arginase (hArginase) I is seen to be up-regulated in many diseases and is a potential therapeutic target for many diverse indications. Previous reports of crystallization and structure determination of hArginase have always included inhibitors of the enzyme: here, the first case of a true apo crystal form of the enzyme which is suitable for small-molecule soaking is reported. The crystals belonged to space group P2(1)2(1)2(1) and have approximate unit-cell parameters a=53, b=67.5, c=250 Å. The crystals showed slightly anisotropic diffraction to beyond 2.0 Å resolution.
精氨酸酶（EC 3.5.3.1）是一种氨基水解酶，作用于L-精氨酸以产生尿素和鸟氨酸。在人类中发现了该酶的两种同种型。I型主要在肝脏中产生，是由35 kDa亚基组成的同三聚体。人精氨酸酶（hArginase）I在许多疾病中被发现上调，是多种适应症的潜在治疗靶点。先前关于hArginase结晶和结构测定的报道总是包含该酶的抑制剂：在此，报道了第一例适用于小分子浸泡的该酶真正无配体晶体形式。晶体属于空间群P2(1)2(1)2(1)，近似晶胞参数a = 53、b = 67.5、c = 250 Å。晶体显示出略微各向异性的衍射，分辨率超过2.0 Å。
