FEBS Letters | |
VAT‐1 from Torpedo is a membranous homologue of zeta crystallin | |
Linial, Michael1  Levius, Orit1  | |
[1] Department of Biological Chemistry, The Alexander Silverman Institute of Life Science, The Hebrew University, Jerusalem 91904, Israel | |
关键词: Electric organ; Lens crystallin; Oxidoreductase; Protein evolution; Synaptic vesicle; SDS; sodium dodecyl sulfate; PAGE; polyacrylamidegel electrophoresis; ADH; alcohol dehydrogenase; FAS; fatty acid ynthase; aa; amino acid; | |
DOI : 10.1016/0014-5793(93)81140-U | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
VAT-1 is a major protein from Torpedo synaptic vesicles. A protein data-base search revealed a striking homology to ξ crystallin from guinea pig lens. The overall amino-acid identity is 27%, and 58% similarity is reached by including conserved substitutions. The highest similarity (60% to 85%) between the two proteins is observed in five discrete domains, which are also conserved in zinc-dependent dehydrogenases, particularly in the alcohol dehydrogenase family. The cofactor-binding domain of oxidoreductases is conserved in VAT-1 and in ξ crystallin. VAT-1 preferably binds NADPH in the presence of zinc. In contrast with its homologous proteins, VAT-1 is an integral membrane protein of synaptic vesicles.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020297304ZK.pdf | 420KB | download |