3150-22-9

Basic information

• Product Name: 4-Methylphenylb-D-galactopyranoside
• Synonyms: 4-Methylphenylb-D-galactopyranoside
• CAS NO: 3150-22-9
• Molecular Formula: C₁₃H₁₈O₆
• Molecular Weight: 270.279
• Mol File: 3150-22-9.mol
• Article Data: 5

Chemical Properties

• Melting Point: 158-161 °C
• Boiling Point: 493.7±45.0 °C(Predicted)
• Appearance: /
• Density: 1.401±0.06 g/cm3(Predicted)
• PKA: 12.85±0.70(Predicted)
• CAS DataBase Reference: 4-Methylphenylb-D-galactopyranoside(CAS DataBase Reference)
• NIST Chemistry Reference: 4-Methylphenylb-D-galactopyranoside(3150-22-9)
• EPA Substance Registry System: 4-Methylphenylb-D-galactopyranoside(3150-22-9)

Safety Data

• Hazardous Substances Data: 3150-22-9(Hazardous Substances Data)

Upstream product

• 3520-64-7 p-methylphenyl 2,3,4,6-tetra-O-acetyl-1-thio-β-D-galactopyranoside 
• 32742-30-6 4-methylphenyl 2,3,4,6-tetra-O-acetyl-α-D-glucopyranoside 
• 604-69-3 β-D-glucose pentaacetate 
• 106-44-5 p-cresol 
• 69-79-4 D-maltose 
• 3520-64-7 p-tolyl-(tetra-O-acetyl-α-D-galactopyranoside) 
• 3068-32-4 1-bromo-1-deoxy-2,3,4,6-tetra-O-acetyl-a-D-galactopyranoside 
• 25878-60-8 D-galactose pentaacetate 

Downstream Products

• 32742-30-6 4-methylphenyl 2,3,4,6-tetra-O-acetyl-α-D-glucopyranoside 

Relevant articles and documents

COMPOUNDS AND METHODS FOR TREATING BACTERIAL INFECTIONS

The present invention is directed to various compounds, compositions, and methods for treating bacterial infections such as urinary tract infections.

Purification, characterization, and gene identification of an α-glucosyl transfer enzyme, a novel type α-glucosidase from Xanthomonas campestris WU-9701

The α-glucosyl transfer enzyme (XgtA), a novel type α-glucosidase produced by Xanthomonas campestris WU-9701, was purified from the cell-free extract and characterized. The molecular weight of XgtA is estimated to be 57 kDa by SDS-PAGE and 60 kDa by gel filtration, indicating that XgtA is a monomeric enzyme. Kinetic properties of XgtA were determined for α-glucosyl transfer and maltose-hydrolyzing activities using maltose as the α-glucosyl donor, and if necessary, hydroquinone as the acceptor. The Vmax value for α-glucosyl transfer activity was 1.3 × 10-2 (mM/s); this value was 3.9-fold as much as that for maltose-hydrolyzing activity. XgtA neither produced maltooligosaccharides nor hydrolyzed sucrose. The gene encoding XgtA that contained a 1614-bp open reading frame was cloned, identified, and highly expressed in Escherichia coli JM109 as the host. Site-directed mutagenesis identified Asp201, Glu270, and Asp331 as the catalytic sites of XgtA, indicating that XgtA belongs to the glycoside hydrolase family 13.

(Halogenomethyl)phenyl &α-D-Glucopyranosides as Enzyme-activated Irreversible Inhibitors of Yeast &α-Glucosidase and Potential Anti-HIV Agents

A range of (halogenomethyl)phenyl α-D-glucopyranosides 2-7, prepared from corresponding methylphenyl glucosides by synthetic manipulation of the aglycone moiety, have been investigated as enzyme-activated irreversible inhibitors of yeast α-glucosidase and