H-D-Tyr-Val-Gly-OH

Description:

The tripeptide H-D-Tyr-Val-Gly-OH can be converted into H-D-Tyr-Val-NH₂ by a secretory granule-associated enzyme activity.Substrate (in combination with ascorbate) for peptidylglycine monooxygenase.

Sequence:

{D-Tyr}VG

General

References

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Name	H-D-Tyr-Val-Gly-OH
Category	Enzyme Substrates and Inhibitors
One Letter Code	{D-Tyr}VG
Three Letter Code	{D-Tyr}{Val}{Gly}
Molecular Weight	337.380
Application	Di- and Tripeptides

Biegel, Annegret, et al. "Three-dimensional quantitative structure− activity relationship analyses of β-lactam antibiotics and tripeptides as substrates of the mammalian H+/peptide cotransporter PEPT1." Journal of medicinal chemistry 48.13 (2005): 4410-4419.

Von Zastrow, Mark, Thomas R. Tritton, and J. David Castle. "Exocrine secretion granules contain peptide amidation activity." Proceedings of the National Academy of Sciences 83.10 (1986): 3297-3301.

Prohaska, Joseph R., and Margaret Broderius. "Plasma peptidylglycine alpha-amidating monooxygenase (PAM) and ceruloplasmin are affected by age and copper status in rats and mice." Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 143.3 (2006): 360-366.

Takahashi, Kenichi, et al. "Expression and characterization of frog peptidylglycine α-hydroxylating monooxygenase." Protein expression and purification 27.1 (2003): 35-41.

Miller, Laura Aaron, et al. "Glutathione, S-substituted glutathiones, and leukotriene C4 as substrates for peptidylglycine α-amidating monooxygenase." Archives of biochemistry and biophysics 412.1 (2003): 3-12.