product name
L -脯氨酸对硝基苯胺 三氟乙酸盐, prolyl aminopeptidase substrate
质量水平
检测方案
≥99% (TLC)
形式
powder
技术
ligand binding assay: suitable
颜色
white to yellow
储存温度
2-8°C
SMILES字符串
OC(=O)C(F)(F)F.[O-][N+](=O)c1ccc(NC(=O)[C@@H]2CCCN2)cc1
InChI
1S/C11H13N3O3.C2HF3O2/c15-11(10-2-1-7-12-10)13-8-3-5-9(6-4-8)14(16)17;3-2(4,5)1(6)7/h3-6,10,12H,1-2,7H2,(H,13,15);(H,6,7)/t10-;/m0./s1
InChI key
KYRVEVYREUUAKH-PPHPATTJSA-N
一般描述
脯氨酸对硝基苯胺 (p-pNA) 是脯氨酰氨肽酶（脯氨酸亚氨基肽酶）的比色底物，脯氨酸亚氨基肽酶是一种从小肽 N -末端释放脯氨酸的酶。
应用
L-脯氨酸对硝基苯胺三氟乙酸盐还用作单肽底物，测定纤化肽催化剂PC4的氨基分解活性。
脯氨酸对硝基苯胺(p-pNA)已用作卷心菜来源脯氨酰氨肽酶（脯氨酸亚氨基肽酶）的底物。
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
Hongyu Yang et al.
World journal of microbiology & biotechnology, 32(11), 176-176 (2016-09-16)
Prolyl aminopeptidases are specific exopeptidases that catalyze the hydrolysis of the N-terminus proline residue of peptides and proteins. In the present study, the prolyl aminopeptidase gene (pap) from Aspergillus oryzae JN-412 was optimized through the codon usage of Pichia pastoris.
Margarita Marinova et al.
Protein and peptide letters, 16(2), 207-212 (2009-02-10)
Chick-pea (Cicer arietinum L.) cotyledons are unique source of aminopeptidase - 8-9 U/g cotyledons was observed using L-leucine-p-nitroanilide as substrate. The aminopeptidase was purified (65 kDa, pI 4.8 ) reaching a specific activity of 220 U/mg at pH 7.0-7.2 and
Margarita Marinova et al.
Zeitschrift fur Naturforschung. C, Journal of biosciences, 63(1-2), 105-112 (2008-04-05)
Aminopeptidase, preferring phenylalanine-p-nitroanilide as substrate, and proline iminopeptidase, highly-specific for proline-p-nitroanilide, were isolated from cabbage leaves (Brassica oleraceae var. capitata). As pH optima, 7.2-7.5 for aminopeptidase activity and 8.0-8.5 for proline iminopeptidase were determined. Both peptidases were strongly inhibited by
Kazuyuki Hiwatashi et al.
Bioscience, biotechnology, and biochemistry, 68(6), 1395-1397 (2004-06-25)
We have found a novel prolyl aminopeptidase in Grifola frondosa. The enzyme was purified by DEAE-Sepharose CL-6B, Butyl-Toyopearl, Sephacryl S-100, and Mono-Q column chromatographies. The purified enzyme exists as a dimer and gives high activity toward L-proline-p-nitroanilide. The enzyme was
Yoke-Ming Wong et al.
Biomacromolecules, 17(10), 3375-3385 (2016-09-20)
Amyloid fibers are classified as a new generation of tunable bionanomaterials that exhibit new functions related to their distinctive characteristics, such as their universality, tunability, and stiffness. Here, we introduce the catalytic residues of serine protease into a peptide catalyst
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