Characteristics of an aminopeptidase from Japanese cedar (Cryptomeria japonica) pollen.
Characteristics of an aminopeptidase from Japanese cedar (Cryptomeria japonica) pollen.
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DOI：
10.1021/jf047794b
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发表时间：
2005-05
影响因子：
6.1
通讯作者：
H. Nagata;T. Takei;Ryoko Kojima;Y. Kodera;H. Nishimura;Y. Inada;A. Matsushima
中科院分区：
文献类型：
--
作者：
H. Nagata;T. Takei;Ryoko Kojima;Y. Kodera;H. Nishimura;Y. Inada;A. Matsushima
A peptidase from Japanese cedar pollen, Jc-peptidase, was clarified to preferentially hydrolyze an MCA substrate of Phe-MCA (L-phenylalanyl-4-methylcoumaryl-7-amide). This study examined substrate specificities of Jc-peptidase using oligopeptides. Jc-peptidase hydrolyzed Phe-Phe and Tyr-Phe effectively and hydrolyzed Leu-Phe, Met-Phe, and Arg-Phe moderately. Other substrates such as Ala-Phe, Asp-Phe, and Pro-Phe were not hydrolyzed with the peptidase. Results obtained with a series of aminoacyl-Phe peptides were compatible with the facts obtained for MCA substrates except for Arg-MCA. Effects of amino acid residues in the P1' position were also examined using Phe-amino acids. An N-terminal phenylalanine residue was actually released from bioactive peptides such as molluscan cardioexcitatory neuropeptide (FMRF-NH(2)). Because the activity was inhibited with Zn(2+) and EDTA, Jc-peptidase was inferred to belong to the metalloproteases. The N-terminal amino acid sequence was determined to be APIGVQLEIEENYVHMYNGF and an internal sequence to be EIFAATFNVDEETEA, but no homology with other proteins was found.
