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辅脂酶
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辅脂酶(Colipase) 是一种蛋白质辅酶,可提升胰脂酶(英语:lipase)的酵素活性。本蛋白的前体前辅脂酶(procolipase)由胰腺所分泌,此时并没有酵素活性。前辅脂酶进入肠道后,会被胰蛋白酶分解为辅脂酶,此时方有功能。辅脂酶的功能是为了防止胆盐在十二指肠内抑制脂肪酶水解三酸甘油酯。
Quick Facts 辅脂酶, 识别号 ...
辅脂酶 | |||||||||||||||||||||||||
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识别号 | |||||||||||||||||||||||||
别名 | CLPS;, entrez:1208, colipase | ||||||||||||||||||||||||
外部ID | OMIM:120105 MGI:88421 HomoloGene:1383 GeneCards:CLPS | ||||||||||||||||||||||||
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物种 | 人类 | 小鼠 | |||||||||||||||||||||||
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蛋白序列 | |||||||||||||||||||||||||
基因位置(UCSC) | Chr 6: 35.79 – 35.8 Mb | Chr 17: 28.78 – 28.78 Mb | |||||||||||||||||||||||
PubMed查找 | [3] | [4] | |||||||||||||||||||||||
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在人类中,辅脂酶由 CLPS 基因翻译而得。[5]
蛋白质结构域
辅脂酶是胰脂酶可有效提升胰脂酶的功能,影响人体吸收三酸甘油脂的能力。辅脂酶会与胰脂酶的无酵素活性的C端结合,稳定其激活态。辅脂酶还能提高其结合位点的疏水性。 相关的蛋白质结构研究已解开其单体及复合体立体结构的功能[6][7]。
辅脂酶是一个具有五个保守双硫键的小型蛋白质。其结构类似Dickkopf蛋白[7]。
More information Colipase N-terminal domain, 鉴定 ...
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Quick Facts Colipase C-terminal domain, 鉴定 ...
Colipase C-terminal domain | |||||||||
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![]() solution structure of porcine pancreatic procolipase as determined from 1h homonuclear two-and three-dimensional nmr | |||||||||
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标志 | Colipase_C | ||||||||
Pfam | PF02740(旧版) | ||||||||
InterPro(英语:InterPro) | IPR017914 | ||||||||
PROSITE(英语:PROSITE) | PDOC00111 | ||||||||
SCOP(英语:Structural Classification of Proteins) | 1lpb / SUPFAM | ||||||||
CDD(英语:Conserved Domain Database) | cd00039 | ||||||||
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参见
- Enterostatin(英语:Enterostatin)
参考文献
- Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
- Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
- Davis RC, Xia YR, Mohandas T, Schotz MC, Lusis AJ. Assignment of the human pancreatic colipase gene to chromosome 6p21.1 to pter. Genomics. May 1991, 10 (1): 262–5. PMID 2045105. doi:10.1016/0888-7543(91)90509-D.
- Lowe ME. Structure and function of pancreatic lipase and colipase. Annu. Rev. Nutr. 1997, 17: 141–158. PMID 9240923. doi:10.1146/annurev.nutr.17.1.141.
- Verger R, van Tilbeurgh H, Cambillau C, Bezzine S, Carriere F. Colipase: structure and interaction with pancreatic lipase. Biochim. Biophys. Acta. 1999, 1441 (2–3): 173–184. PMID 10570245. doi:10.1016/s1388-1981(99)00149-3.
- Egloff MP, Marguet F, Buono G, Verger R, Cambillau C, van Tilbeurgh H. The 2.46 A resolution structure of the pancreatic lipase-colipase complex inhibited by a C11 alkyl phosphonate. Biochemistry. March 1995, 34 (9): 2751–62. PMID 7893686. doi:10.1021/bi00009a003.