Amino-acid sequences of heme-linked, histidine-containing peptides of five peroxidases from horseradish and turnip.

Amino-acid sequences of heme-linked, histidine-containing peptides of five peroxidases from horseradish and turnip.
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来自辣根和萝卜的五种过氧化物酶的血红素连接的含组氨酸肽的氨基酸序列。

DOI:
10.1111/j.1432-1033.1977.tb11325.x
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发表时间:
1977
期刊:
European journal of biochemistry
影响因子:
--
通讯作者:
Gilbert Mazza
Gilbert Mazza
中科院分区:
--
文献类型:
--
作者:
K. Welinder;Gilbert Mazza

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在之前的一篇论文中,我们通过肽图谱研究对萝卜和辣根过氧化物酶同工酶C的五种植物过氧化物酶P1、P2、P3和P7进行了表征,只发现其中存在两个高度同源的序列。两者都含有组氨酸。这一发现支持了以前的建议,即在过氧化物酶血红素前列腺组附近有两个组氨酸序列。本文报道了芜菁过氧化物酶的组氨酸残基周围的氨基酸序列。e.对辣根过氧化物酶C的含组氨酸氨基酸序列进行了分析,并与辣根过氧化物酶C的含组氨酸氨基酸序列进行比较。在这些组氨酸附近残基的取代是罕见的,但随着距离的增加而更丰富。P1、P2、P3和辣根过氧化物酶C的可能的远端序列在位置40和42处都含有两个组氨酸残基。然而,在P7中,残基40是苯丙氨酸,这一取代可能对其异常的理化和酶性质很重要。芜菁过氧化物酶同工酶的胰蛋白酶的凝胶过滤图谱证实了它们先前的分类为P1和P3组以及不同的P7酶,但进一步证明了在P1、P2和P3过氧化物酶中存在几个碳水化合物附着位点,如在辣根过氧化物酶C中,其具有8个位点。P7就有这样一个网站。
In a previous paper we have characterized five plant peroxidases, P1, P2, P3 and P7 of turnip and horseradish isoperoxidase C by peptide mapping studies, and only found two highly homologous sequences present in all. Both contained histidine. The findings supported previous suggestions of two histidine sequences nearthe peroxidase heme prostetic group. In the present paper we present the amino acid sequences around the histidine residues of all four turnip peroxidases, i. e. of 25 residues around the histidine proximal to heme, and 34 residues around the probably distally located histidine, and compare them with the histidine-containing sequences of the complete amino acid sequence of horseradish isoperoxidase C. Substitutions of residues are rare close to these histidines, but more abundant with greater distances. The probably distal sequences of P1, P2, P3, and horseradish peroxidase C all contain two histidine residues, at positions 40 and 42. In P7, however, residue 40 is phenylalanine, a substitution presumably important to its abnormal physio-chemical and enzymic properties. Gel filtration profiles of tryptic digests of the turnip isoperoxidases confirm their previous classification into a P1, and P3 group and a distinct P7 enzyme, but further prove the presence of several sites of carbohydrate attachment in P1, P2 and P3 peroxidases, like in horeseradish peroxidase C which has eight sites. P7 has one such site.