一般描述
Aminopeptidase I from Streptomyces griseus is a thermostable enzyme with Glu131 and Tyr246 as key active site residues.
应用
Aminopeptidase I from Streptomyces griseus has been used:
- to test the biochar exposure effect on the enzyme activity
- in circular dichroism (CD) spectroscopy studies
- as a positive control in p-nitroanilide degradation assay
生化/生理作用
Aminopeptidase I from S. griseus has a fairly broad specificity, being able to remove the N-terminal residue of most proteins, except where the penultimate residue is an imino acid. It contains two Zn2+ binding sites. Aminopeptidase I from S. griseus is inhibited by 1,10-phenanthroline and is activated six-fold by Ca2+, which also stabilizes it against heat inactivation. This monomeric zinc metalloprotein has an isoelectric point (pI) of 5.4.
Aminopeptidase I may also be used as a reagent in the assay of endoprotease activities with a synthetic substrate in a two-stage assay. In the first stage, the endoprotease cleaves a peptide, such as Z-Y-X-Leu-p-nitroanilide, with the X, Y, and Z residues being chosen according to the specificity of the endoprotease.
包装
Package size based on protein content.
单位定义
One unit will hydrolyze 1.0 μmole of L-leucine-p-nitroanilide to L-leucine and p-nitroaniline per min at pH 8.0, 25 °C and 3.0 mM substrate concentration.
外形
Contains calcium acetate
制备说明
Reconstitute in 20 mM tricine, pH 8.0, with 0.05% bovine serum albumin. Dilute the enzyme with the reconstitution buffer to 0.15-0.3 U/mL for a working concentration. Solutions should be prepared fresh prior to use.
其他说明
Endopeptidase contaminant: Not more than: 0.01 U/mg protein (as μmole tyrosine equivalent per min released from casein.)
警示用语：
Danger
危险分类
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
靶器官
Respiratory system
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
法规信息
常规特殊物品
[Cytoplasm to vacuole targeting pathway in yeast].
Takahiro Shintani
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 51(10 Suppl), 1480-1483 (2006-08-23)
Bonnie K Baxter et al.
The Journal of biological chemistry, 280(47), 39067-39076 (2005-09-28)
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 their receptor, Atg19p
Jason L Parsons et al.
The FEBS journal, 272(22), 5753-5763 (2005-11-11)
Ionizing radiation, oxidative stress and endogenous DNA-damage processing can result in a variety of single-strand breaks with modified 5' and/or 3' ends. These are thought to be one of the most persistent forms of DNA damage and may threaten cell
Wakana Adachi et al.
Acta crystallographica. Section F, Structural biology and crystallization communications, 63(Pt 3), 200-203 (2007-03-03)
The vacuole hydrolase aminopeptidase 1 (Ape1) is a cargo protein transported to the vacuole by the cytosol-to-vacuole targeting (Cvt) pathway during conditions of growth and by autophagy during conditions of starvation. After transport to the vacuole, Ape1 is processed into
Claudine Kraft et al.
Nature cell biology, 10(5), 602-610 (2008-04-09)
Eukaryotic cells use autophagy and the ubiquitin-proteasome system (UPS) as their major protein degradation pathways. Whereas the UPS is required for the rapid degradation of proteins when fast adaptation is needed, autophagy pathways selectively remove protein aggregates and damaged or
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