H-Glu-Ala-Leu-Phe-Gln-pNA, with the CAS number 198551-00-7, is a synthetic peptide that consists of a sequence of amino acids, specifically glutamic acid (Glu), alanine (Ala), leucine (Leu), phenylalanine (Phe), and glutamine (Gln), with a para-nitroanilide (pNA) moiety. This compound is often utilized in biochemical assays, particularly in the study of proteolytic enzymes, due to its ability to release the pNA chromophore upon cleavage by proteases. The presence of the pNA group allows for easy spectrophotometric detection, making it a valuable tool in enzyme kinetics and activity studies. The peptide's structure contributes to its stability and specificity in enzymatic reactions. Additionally, the sequence of amino acids can influence the peptide's interactions with enzymes, affecting its substrate specificity and reaction rates. Overall, H-Glu-Ala-Leu-Phe-Gln-pNA serves as an important model compound in biochemical research, particularly in the fields of enzymology and peptide chemistry.

H-Glu-Ala-Leu-Phe-Gln-pNA

198551-00-7: H-Glu-Ala-Leu-Phe-Gln-pNA, with the CAS number 198551-00-7, is a synthetic peptide that consists of a sequence of amino acids, specifically glutamic acid (Glu), alanine (Ala), leucine (Leu), phenylalanine (Phe), and glutamine (Gln), with a para-nitroanilide (pNA) moiety. This compound is often utilized in biochemical assays, particularly in the study of proteolytic enzymes, due to its ability to release the pNA chromophore upon cleavage by proteases. The presence of the pNA group allows for easy spectrophotometric detection, making it a valuable tool in enzyme kinetics and activity studies. The peptide's structure contributes to its stability and specificity in enzymatic reactions. Additionally, the sequence of amino acids can influence the peptide's interactions with enzymes, affecting its substrate specificity and reaction rates. Overall, H-Glu-Ala-Leu-Phe-Gln-pNA serves as an important model compound in biochemical research, particularly in the fields of enzymology and peptide chemistry.

The substrate EALFQ-pNA representing the 2C/3A cleavage site of human rhinovirus-14 (HRV-14) polyprotein was hydrolyzed by human rhinovirus-14 3C protease, which represents an attractive target for antiviral drug development. It exhibited a kcat/Km value of 840 M⁻¹s⁻¹.

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CAS 198551-00-7

H-Glu-Ala-Leu-Phe-Gln-pNA

H-Glu-Ala-Leu-Phe-Gln-pNA

Ref: 01-4028277

H-Glu-Ala-Leu-Phe-Gln-pNA trifluoroacetate salt

Ref: 3D-FG110808