FERROCHELATASE: THE CONVERGENCE OF THE PORPHYRIN BIOSYNTHESIS AND IRON TRANSPORT PATHWAYS.
FERROCHELATASE: THE CONVERGENCE OF THE PORPHYRIN BIOSYNTHESIS AND IRON TRANSPORT PATHWAYS.
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DOI：
10.1142/s108842461100332x
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发表时间：
2011
影响因子：
1.5
通讯作者：
Ferreira GC
中科院分区：
文献类型：
--
作者：
Hunter GA;Al-Karadaghi S;Ferreira GC
亚铁螯合酶（也称为PPIX亚铁螯合酶;酶委员会编号4.9.9.1.1）催化亚铁插入PPIX以形成血红素。该反应结合了几乎所有生物体中卟啉合成和铁转运的生化同步途径。铁螯合酶是一个进化上多样化的酶家族，已知不超过6个活性位点残基完全保守。超过30种不同的晶体结构，包括许多结合金属离子或卟啉，极大地增加了我们对铁螯合酶结构和功能的理解。一般认为，亚铁离子在体内直接被引导至亚铁螯合酶，但是尽管在该领域最近取得了许多进展，但可疑的伴侣蛋白的身份仍然不确定。鉴定一个保守的金属离子结合位点的基础上的活性位点裂缝可能是一个重要的线索，铁螯合酶如何获得铁，并在运输过程中催化去溶剂化的催化位点完成血红素合成。
Ferrochelatase (also known as PPIX ferrochelatase; Enzyme Commission number 4.9.9.1.1) catalyzes the insertion of ferrous iron into PPIX to form heme. This reaction unites the biochemically synchronized pathways of porphyrin synthesis and iron transport in nearly all living organisms. The ferrochelatases are an evolutionarily diverse family of enzymes with no more than six active site residues known to be perfectly conserved. The availability of over thirty different crystal structures, including many with bound metal ions or porphyrins, has added tremendously to our understanding of ferrochelatase structure and function. It is generally believed that ferrous iron is directly channeled to ferrochelatase in vivo, but the identity of the suspected chaperone remains uncertain despite much recent progress in this area. Identification of a conserved metal ion binding site at the base of the active site cleft may be an important clue as to how ferrochelatases acquire iron, and catalyze desolvation during transport to the catalytic site to complete heme synthesis.