C-terminal alpha-amidating enzyme and process for production and

Details C-terminal alpha-amidating enzyme and process for production and C-terminal alpha-amidating enzyme and process for production and

1987-06-05

1990-05-01

Wiseman, Thomas G.

Chemistry: molecular biology and microbiology

Micro-organism, tissue cell culture or enzyme using process...

Preparing nitrogen-containing organic compound

435189, 435228, 435 681, C12P 1302, C12P 2100, C12N 902, C12N 980

Patent

active

049217976

ABSTRACT:
C-terminal .alpha.-amidating enzyme preparations, including preparations AE-I, AE-II, AE-IIa and AE-IIb, from the skin of Xenopus laevis, wherein all components can convert a peptide having a glycine residue at its C-terminal to a C-terminal amidated peptide lacking the glycine residue, and have a common N-terminal amino acid sequence represented by Ser-Leu-Ser---, and AE-I and AE-IIa have a molecular weight of about 39,000, AE-IIb has a molecular weight of about 34,000, and AE-II comprises two components having molecular weight of about 39,000 and 34,000; a process for production of the above-mentioned enzyme preparations; and a process for .alpha.-amidation of a peptide by using the above mentioned enzyme preparations.

REFERENCES:
patent: 4708934 (1987-11-01), Gilligan et al.
Murthy, A. S. N. et al. (1986), J. Biol. Chem. 261(4), 1815-1822.
Mollay, C. et al. (1986), FEBS Lett. 202(2), 251-254.
Mizuno, K. et al. (1986), Biochem. Biophys. Res. Commun. (1986), 137(3), 984-991.
A. F. Bradbury et al., Nature, vol. 298, pp. 686-688 (1982).
B. A. Eipper et al., PNAS, vol. 80, pp. 5144-5148 (1983).
I. Husain et al., FEBS Letters, vol. 152, pp. 277-281 (1983).
J. S. Kizer et al., PNAS, vol. 81, pp. 3228-3232 (1984).

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