N5885
4-Nitrophenyl α-D-maltoside
glycosidase substrate
别名:
4-Nitrophenyl a-D-maltopyranoside, 4-Nitrophenyl alpha-D-maltoside
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关于此项目
经验公式（希尔记法）:
C18H25NO13
化学文摘社编号:
分子量:
463.39
MDL编号:
UNSPSC代码:
12352204
PubChem化学物质编号:
NACRES:
NA.32
质量水平
方案
≥99% (TLC)
表单
powder
溶解性
water: 49.00-51.00 mg/mL, clear, colorless to light yellow
储存温度
−20°C
SMILES字符串
O[C@@H]1[C@@H](O)[C@H](O[C@@]2([H])O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@@H](CO)O[C@@H]1OC3=CC=C([N+]([O-])=O)C=C3
InChI
1S/C18H25NO13/c20-5-9-11(22)12(23)14(25)18(30-9)32-16-10(6-21)31-17(15(26)13(16)24)29-8-3-1-7(2-4-8)19(27)28/h1-4,9-18,20-26H,5-6H2
InChI key
IAYJZWFYUSNIPN-UHFFFAOYSA-N
储存分类代码
11 - Combustible Solids
WGK
WGK 3
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
涉药品监管产品
K Omichi et al.
Journal of biochemistry, 107(4), 546-549 (1990-04-01)
Human non-salivary, non-pancreatic alpha-amylase (yHXA) is the gene product of a newly found human alpha-amylase gene expressed in yeast. Its mode of action on a fluorogenic derivative of p-nitrophenyl alpha-maltopentaoside, FG5P (FG-G-G-G-G-P), was examined at various pH values to elucidate
K Omichi et al.
Journal of biochemistry, 100(5), 1353-1358 (1986-11-01)
p-Nitrophenyl O-6-deoxy-6-[(2-pyridyl)amino]-alpha-D-glucopyranosyl-(1----4)-O-alpha- D-glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-O-alpha-D- glucopyranosyl-(1----4)-alpha-D-glucopyranoside (FG5P) is hydrolyzed by human pancreatic a-amylase (HPA) or salivary alpha-amylase (HSA) to O-6-deoxy-6-[(2-pyridyl)amino]-alpha-D- glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-D-glucose (FG3) and p-nitrophenyl alpha-maltoside or to O-6-deoxy-6-[(2-pyridyl)amino]-alpha-D-glucopyranosyl-(1----4)-O-alpha- D-glucopyranosyl-(1----4)-O-alpha-D-glucopyranosyl-(1----4)-D-glucose (FG4) and p-nitrophenyl alpha-glucoside. The use of alpha-D-glucosidase (maltase) [EC 3.2.1.20] of Saccharomyces
C C Tseng et al.
Archives of oral biology, 44(2), 119-127 (1999-04-17)
Human salivary alpha-amylase participates in the initial digestion of starch and may be involved in the colonization of viridans streptococci in the mouth. To elucidate the role of histidine residues located near the starch-binding site on the streptococcal-binding activity, the
M Reyes et al.
Journal of bacteriology, 165(3), 918-922 (1986-03-01)
In wild-type Escherichia coli the activity of the maltose transport system is dependent on a periplasmic maltose-binding protein. It has been possible, however, to isolate mutants in which transport activity is mediated by the membrane components of the system and
E H Ajandouz et al.
Biochimica et biophysica acta, 1159(2), 193-202 (1992-09-23)
Isoforms AMY1, AMY2-1 and AMY2-2 of barley alpha-amylase were purified from malt. AMY2-1 and AMY2-2 are both susceptible to barley alpha-amylase/subtilisin inhibitor. The action of these isoforms is compared using substrates ranging from p-nitrophenylmaltoside through p-nitrophenylmaltoheptaoside. The kcat/Km values are
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