Abstract:
:Various proteins sharing thioredoxin (Trx)-like active site sequences (Cys-Xxx-Xxx-Cys) have been found and classified in the Trx superfamily. Among them, transmembrane Trx-related protein (TMX) was recently identified as a novel protein possessing an atypical active site sequence, Cys-Pro-Ala-Cys. In the present study, we describe the properties of this membranous Trx-related molecule. Endogenous TMX was detected as a protein of approximately 30 kDa with a cleavable signal peptide. TMX was enriched in membrane fractions and exhibited a similar subcellular distribution with calnexin localized in the endoplasmic reticulum (ER). The examination of membrane topology of TMX suggested that the N-terminal region containing the Trx-like domain was present in the ER lumen, where protein disulfide isomerase (PDI) was found to assist protein folding. Recombinant TMX showed PDI-like activity to refold scrambled RNase. These results indicate the possibility that TMX can modify certain molecules with its oxidoreductase activity and be involved in the redox regulation in the ER.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Matsuo Y,Nishinaka Y,Suzuki S,Kojima M,Kizaka-Kondoh S,Kondo N,Son A,Sakakura-Nishiyama J,Yamaguchi Y,Masutani H,Ishii Y,Yodoi Jdoi
10.1016/j.abb.2003.11.003subject
Has Abstractpub_date
2004-03-01 00:00:00pages
81-7issue
1eissn
0003-9861issn
1096-0384pii
S0003986103005940journal_volume
423pub_type
杂志文章abstract::We have studied the effectiveness of polyprenyl-P-mannose and polyprenol-P-glucose as donor substrates for the dolichyl-P-mannose:Man5(GlcNAc)2-PP-dolichol mannosyltransferase and the dolichyl-P-glucose:Man9(GlcNAc)2-PP-dolichol glucosyltransferase, respectively. The polyprenol moiety differs from dolichol only in the...
journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
doi:10.1006/abbi.1996.0547
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pub_type: 杂志文章
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abstract::CYP119 from Sulfolobus solfataricus is the first well-characterized thermophilic cytochrome P450 enzyme. The endogenous substrate for this enzyme is not known but it hydroxylates lauric acid in a reaction supported by surrogate mesophilic electron donors. However, reconstitution of a high-temperature catalytic system ...
journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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更新日期:1987-05-15 00:00:00