Molecular characterization of a catalase from Hydra vulgaris.
Molecular characterization of a catalase from Hydra vulgaris.
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DOI：
10.1016/j.gene.2012.04.015
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发表时间：
2012-06-15
期刊：
影响因子：
3.5
通讯作者：
Phillips TD
中科院分区：
文献类型：
--
作者：
Dash B;Phillips TD
Catalase, an antioxidant and hydroperoxidase enzyme protects the cellular environment from harmful effects of hydrogen peroxide by facilitating its degradation to oxygen and water. Molecular information on a cnidarian catalase and/or peroxidase is, however, limited. In this work an apparent full length cDNA sequence coding for a catalase (HvCatalase) was isolated from Hydra vulgaris using 3’- and 5’- (RLM) RACE approaches. The 1859 bp HvCatalase cDNA included an open reading frame of 1518 bp encoding a putative protein of 505 amino acids with a predicted molecular mass of 57.44 kDa. The deduced amino acid sequence of HvCatalase contained several highly conserved motifs including the heme-ligand signature sequence RLFSYGDTH and the active site signature FXRERIPERVVHAKGXGA. A comparative analysis showed the presence of conserved catalytic amino acids [His(71), Asn(145), and Tyr(354)] in HvCatalase as well. Homology modeling indicated the presence of the conserved features of mammalian catalase fold. Hydrae exposed to thermal, starvation, metal and oxidative stress responded by regulating its catalase mRNA transcription. These results indicated that the HvCatalase gene is involved in the cellular stress response and (anti)oxidative processes triggered by stressor and contaminant exposure.
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DOI：
10.1046/j.1432-1327.1998.2550703.x
发表时间：
1998-08-01
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
Brennecke, T;Gellner, K;Bosch, TCG
通讯作者：
Bosch, TCG
影响因子：
4.5
作者：
Dissanayake, Awantha;Galloway, Tamara S.;Jones, Malcolm B.
通讯作者：
Jones, Malcolm B.
影响因子：
3.2
作者：
HAND, AR
通讯作者：
HAND, AR
影响因子：
3.2
作者：
ALLGOOD, GS;PERRY, JJ
通讯作者：
PERRY, JJ
影响因子：
3.5
作者：
Kumar, Manoj;Kumari, Puja;Jha, Bhavanath
通讯作者：
Jha, Bhavanath