SUC-ALA-ALA-PRO-PHE-PNA Chemical Properties

storage temp. 

-20°C

solubility 

DMF: 25 mg/mL, clear, light yellow

form 

White to off-white solid

color 

White to off-white

BRN 

4289896

Sequence

{Suc}-Ala-Ala-Pro-Phe-{pNA}

InChIKey

LKDMKWNDBAVNQZ-UHYNAWRVNA-N

SMILES

N1(CCC[C@H]1C(=O)N[C@H](C(=O)NC1=CC=C([N+]([O-])=O)C=C1)CC1=CC=CC=C1)C(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)CCC(=O)O |&1:4,8,30,35,r|

Safety Information

Safety Statements 

22-24/25

WGK Germany 

3

F 

10

HS Code 

2933998090

MSDS

• Language:English Provider:SigmaAldrich

SUC-ALA-ALA-PRO-PHE-PNA Usage And Synthesis

Description

Suc-AAPF-pNA is a chromogenic substrate that can be cleaved by cathepsin G (K_m = 1.7 mM), subtilisins, chymotrypsin (K_m = 60 μM), chymase (K_m = 4 mM), and cyclophilin, but not neutrophil elastase. Release of p-nitroanilide is monitored at 405-410 nm. This substrate can be used for inhibitor screening and kinetic analysis.

Uses

N-Succinyl-Ala-Ala-Pro-Phe p-nitroanilide has been used as a substrate to determine chymotrypsin activity.

Biochem/physiol Actions

N-succinyl-Ala-Ala-Pro-Phe p-nitroanilide is a substrate for subtilisin and proteases.

References

[1] K. NAKAJIMA. Mapping the extended substrate binding site of cathepsin G and human leukocyte elastase. Studies with peptide substrates related to the alpha 1-protease inhibitor reactive site.[J]. The Journal of Biological Chemistry, 1979, 107 1: 4027-4032. DOI: 10.1016/s0021-9258(18)50690-6
[2] J ERMOLIEFF. Heparin protects cathepsin G against inhibition by protein proteinase inhibitors.[J]. The Journal of Biological Chemistry, 1994, 269 47: 29502-29508.
[3] JAMES L. KOFRON. Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay[J]. Biochemistry Biochemistry, 1991, 30 25: 6127-6134. DOI: 10.1021/bi00239a007
[4] H NAKAKUBO. Secretory production of recombinant human chymase as an active form in Pichia pastoris.[J]. Yeast, 2000, 16 4: 315-323. DOI: 10.1002/1097-0061(20000315)16:4<315::aid-yea527>3.0.co;2-4

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