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Gene Review

Bace1  -  beta-site APP cleaving enzyme 1

Rattus norvegicus

Synonyms: ASP2, Asp 2, Aspartyl protease 2, Bace, Beta-secretase 1, ...
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High impact information on Bace1

  • Using nondenaturating immunoprecipitation and immunoblotting procedures, other endosomal aspartic acid proteases such as cathepsin E and beta-site amyloid precursor protein-cleaving enzyme (BACE) were ruled out as candidate enzymes for the endosomal degradation of internalized insulin [1].
  • Directed mutagenesis of GATA-1 elements led to altered luciferase expression, indicating that these sites are involved in the regulation of BACE1 transcription [2].
  • By capillary LC-MS and tandem MS, we show that, in approximately one third of the Calpha and Cbeta enzyme populations from cattle, pig, rabbit, and rat striated muscle, Asn 2 is deamidated to Asp 2 [3].
  • Asp2, Trp4 and the C-terminal glycinamide have been challenged by classical amino acid substitutions with the aim of elucidating the structural requirements responsible for NK2 subtype selectivity [4].
  • Although JMV-180 differs from CCK-8 by having an Asp-2 phenylethylester, rather than an Asp-phenylalanine amide, it is unlikely that these differences in the carboxyl terminus are important in determining which second-messenger systems will be activated [5].


  1. Endosomal proteolysis of internalized insulin at the C-terminal region of the B chain by cathepsin D. Authier, F., Metioui, M., Fabrega, S., Kouach, M., Briand, G. J. Biol. Chem. (2002) [Pubmed]
  2. Cloning and expression of the rat BACE1 promoter. Lange-Dohna, C., Zeitschel, U., Gaunitz, F., Perez-Polo, J.R., Bigl, V., Rossner, S. J. Neurosci. Res. (2003) [Pubmed]
  3. A conserved deamidation site at Asn 2 in the catalytic subunit of mammalian cAMP-dependent protein kinase detected by capillary LC-MS and tandem mass spectrometry. Jedrzejewski, P.T., Girod, A., Tholey, A., König, N., Thullner, S., Kinzel, V., Bossemeyer, D. Protein Sci. (1998) [Pubmed]
  4. Structure-activity relationship study of R396, an NK2 tachykinin antagonist selective for the NK2B receptor subtype. Rovero, P., Astolfi, M., Manzini, S., Jukic, D., Rouissi, N., Maggi, C.A., Regoli, D. Neuropeptides (1992) [Pubmed]
  5. Structural requirements of CCK analogues to differentiate second messengers and pancreatic secretion. Tsunoda, Y., Yoshida, H., Owyang, C. Am. J. Physiol. (1996) [Pubmed]
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