STRUCTURAL RELATIONSHIP BETWEEN THE MAMMALIAN FE(III)-FE(II) AND THE FE(III)-ZN(II) PLANT PURPLE ACID-PHOSPHATASES

被引：83

作者：

KLABUNDE, T ^{[1
]}

STRATER, N ^{[1
]}

KREBS, B ^{[1
]}

WITZEL, H ^{[1
]}

机构：

[1] UNIV MUNSTER, INST BIOCHEM, D-48149 MUNSTER, GERMANY

来源：

FEBS LETTERS | 1995年 / 367卷 / 01期

关键词：

PURPLE ACID PHOSPHATASES; SEQUENCE ALIGNMENT; STRUCTURE PREDICTION; ANCESTOR ENZYME; OXYGEN ACTIVATION;

D O I：

10.1016/0014-5793(95)00536-I

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The primary structure of uteroferrin (Uf), a 35 kDa monomeric mammalian purple acid phosphatase (PAP) containing a Fe(III)-Fe(II) center, has been compared with the sequence of the homodimeric 111 kDa Fe(III)-Zn(II) kidney bean purple acid phosphatase (KBPAP). The alignment suggests that the amino acid residues ligating the dimetal center are identical in Uf and KBPAP, although the geometry of the coordination sphere might slightly differ. Secondary structure predictions indicate that Uf contains two beta alpha beta alpha beta motifs thus resembling the folding topology of the plant enzyme. Guided by the recently determined X-ray structure of KBPAP a tentative model for the mammalian PAP can be constructed.

引用

页码：56 / 60

页数：5

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