FA-Gly-Phe-NH₂

Description:

substrate for thermolysin and the fibrinolytic neutral metalloendopeptidase EM 19000 from Streptococcus faecalis.

Sequence:

3-(2-Furyl)acrylic acid- GF -NH₂

General

References

Comments (0)

Name	FA-Gly-Phe-NH₂
Category	Enzyme Substrates and Inhibitors
One Letter Code	3-(2-Furyl)acrylic acid- GF -NH₂
Three Letter Code	3-(2-Furyl)acrylic acid-{Gly}{Phe}-NH₂
Molecular Weight	341.370
Application

He, Hai-Lun, et al. "Structural and functional characterization of mature forms of metalloprotease E495 from Arctic sea-ice bacterium Pseudoalteromonas sp. SM495." PloS one 7.4 (2012).

Sabat, Artur J., et al. "Polymorphism, genetic exchange and intragenic recombination of the aureolysin gene among Staphylococcus aureusstrains." BMC microbiology 8.1 (2008): 129.

Zotzel, Jens, et al. "Activated transglutaminase from Streptomyces mobaraensis is processed by a tripeptidyl aminopeptidase in the final step." European journal of biochemistry 270.20 (2003): 4149-4155.

Zotzel, J., P. Keller, and H‐L. Fuchsbauer. "Transglutaminase from Streptomyces mobaraensis is activated by an endogenous metalloprotease." European journal of biochemistry 270.15 (2003): 3214-3222.

de Kreij, Arno, et al. "The effect of changing the hydrophobic S1′ subsite of thermolysin‐like proteases on substrate specificity." European journal of biochemistry 268.18 (2001): 4985-4991.