Native Streptomyces griseus Aminopeptidase I
Native Streptomyces griseus Aminopeptidase I structure
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Common Name | Native Streptomyces griseus Aminopeptidase I | ||
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| CAS Number | 9031-94-1 | Molecular Weight | 245.234 | |
| Density | 1.4±0.1 g/cm3 | Boiling Point | N/A | |
| Molecular Formula | C17H25N7O4.2[HCl] | Melting Point | N/A | |
| MSDS | Chinese USA | Flash Point | N/A | |
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Lack of involvement of CEP adducts in TLR activation and in angiogenesis.
PLoS ONE 9(10) , e111472, (2014) Proteins that are post-translationally adducted with 2-(ω-carboxyethyl)pyrrole (CEP) have been proposed to play a pathogenic role in age-related macular degeneration, by inducing angiogenesis in a Toll Like Receptor 2 (TLR2)-dependent manner. We have investig... |
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Human hAtg2A protein expressed in yeast is recruited to preautophagosomal structure but does not complement autophagy defects of atg2Δ strain.
Acta Biochim. Pol. 58(3) , 365-74, (2011) Yeast Atg2, an autophagy-related protein, is highly conserved in other fungi and has two homologues in humans, one of which is hAtg2A encoded by the hATG2A/KIAA0404 gene. Region of homology between Atg2 and hAtg2A proteins comprises the C-terminal domain. We ... |
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Yeast Mon2p is a highly conserved protein that functions in the cytoplasm-to-vacuole transport pathway and is required for Golgi homeostasis.
J. Cell Sci. 118(Pt 20) , 4751-64, (2005) Although the small Arf-like GTPases Arl1-3 are highly conserved eukaryotic proteins, they remain relatively poorly characterized. The yeast and mammalian Arl1 proteins bind to the Golgi complex, where they recruit specific structural proteins such as Golgins.... |
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Atg19p ubiquitination and the cytoplasm to vacuole trafficking pathway in yeast.
J. Biol. Chem. 280(47) , 39067-76, (2005) The cytoplasm to vacuole (Cvt) trafficking pathway in S. cerevisiae is a constitutive biosynthetic pathway required for the transport of two vacuolar enzymes, aminopeptidase I (Ape1p) and alpha-mannosidase (Ams1p), to the vacuole. Ape1p and Ams1p bind to thei... |
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Yeast aminopeptidase I. Chemical composition and catalytic properties.
Biochim. Biophys. Acta 429(3) , 933-49, (1976) An aminopeptidase (alpha-aminoacyl L-peptide hydrolase, EC 3.4.11.1) was purified to homogeneity from autolysates of brewer's yeast. The enzyme which is responsible for most of the yeast cell's aminopeptidase activity is a glycoprotein containing about 12% of... |
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Self-interaction is critical for Atg9 transport and function at the phagophore assembly site during autophagy.
Mol. Biol. Cell 19(12) , 5506-16, (2008) Autophagy is the degradation of a cell's own components within lysosomes (or the analogous yeast vacuole), and its malfunction contributes to a variety of human diseases. Atg9 is the sole integral membrane protein required in formation of the initial sequeste... |
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Trs85 is required for macroautophagy, pexophagy and cytoplasm to vacuole targeting in Yarrowia lipolytica and Saccharomyces cerevisiae.
Autophagy 1(1) , 37-45, (2005) Yarrowia lipolytica was recently introduced as a new model organism to study peroxisome degradation in yeasts. Transfer of Y. lipolytica cells from oleate/ethylamine to glucose/ammonium chloride medium leads to selective macroautophagy of peroxisomes. To deci... |
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Atg11 links cargo to the vesicle-forming machinery in the cytoplasm to vacuole targeting pathway.
Mol. Biol. Cell 16(4) , 1593-605, (2005) Proteins are selectively packaged into vesicles at specific sites and then delivered correctly to the various organelles where they function, which is critical to the proper physiology of each organelle. The precursor form of the vacuolar hydrolase aminopepti... |
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Identification of a cytoplasm to vacuole targeting determinant in aminopeptidase I.
J. Cell Biol. 132(6) , 999-1010, (1996) Aminopeptidase I (API) is a soluble leucine aminopeptidase resident in the yeast vacuole (Frey, J., and K.H. Rohm. 1978. Biochim. Biophys. Acta. 527:31-41). The precursor form of API contains an amino-terminal 45-amino acid propeptide, which is removed by pro... |
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Molecular cloning and sequencing of genomic DNA encoding aminopeptidase I from Saccharomyces cerevisiae.
J. Biol. Chem. 264(12) , 6979-83, (1989) Yeast aminopeptidase I is a vacuolar enzyme, which catalyzes the removal of amino acids from the NH2 terminus of peptides and proteins (Frey, J., and Rohm, K-H. (1978) Biochim. Biophys. Acta 527, 31-41). A yeast genomic DNA encoding aminopeptidase I was clone... |