人红细胞二磷酸甘油酸变位酶的结晶及初步X射线衍射研究。
Crystallization and preliminary X-ray diffraction studies of the human erythrocyte bisphosphoglycerate mutase.
作者信息
Cherfils J, Rosa R, Garel M C, Calvin M C, Rosa J, Janin J
机构信息
Laboratoire de Biologie Physicochimique, CNRS UA1131, Université Paris-Sud, Orsay, France.
出版信息
J Mol Biol. 1991 Mar 20;218(2):269-70. doi: 10.1016/0022-2836(91)90710-n.
PMID:1826331
Abstract
Bisphosphoglycerate mutase (EC 2.7.5.4) catalyzes the synthesis and breakdown of 2,3-diphosphoglycerate in red cells. The human enzyme, cloned and expressed in Escherichia coli has been crystallized in the rhombohedral space group R32 with a = b = c = 100.4 A and alpha = beta = gamma = 81.2 degrees. The asymmetric unit contains either a dimeric enzyme molecule, or a monomer.
摘要
二磷酸甘油酸变位酶（EC 2.7.5.4）催化红细胞中2,3-二磷酸甘油酸的合成与分解。在大肠杆菌中克隆并表达的人源酶已在菱面体空间群R32中结晶，晶胞参数a = b = c = 100.4 Å，α = β = γ = 81.2°。不对称单元包含一个二聚体酶分子或一个单体。
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