Alpha amidating enzyme

A process according to claim 6 wherein the C-terminal α-amidating enzyme has amino acid sequence (IV) and wherein C represent the amino acid sequence (IV), X represents Ala, Y represents Thr, and Z represents Ala, and D represents the amino acid sequence (X).11.A process according to claim 6 wherein the C-terminal α-amidating enzyme has amino acid sequence (IV) and wherein C represents the amino acid sequence (VI), X represents Ala, Y represents Thr, and Z represents Ala, and D is absent.12.Abstract of EP0299790A C-terminal alpha -amidating enzyme of Xenopus laevis and precursor thereof produced by a recombinant DNA technique; a DNA coding for the enzyme or precursor thereof; a plasmid containing the DNA; a host organism transformed with the plasmid; a process for production of the enzyme using the transformant; and a process for production of a C-terminal alpha -amidated peptide using the enzyme. MIZUNO et al.: "Cloning and sequence of c DNA encoding a peptide C-terminal alpha-amidating enzyme from Xenopus laevis skin" BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, vol. 3, 15th February 1988, pages 1275-1281, Academic Press, Inc.; K.Ohsuye, Kazuhiro (1-6-2 Yamatedai, Ibaraki-shi, Osaka, JP) Kitano, Katsuhiko (2-13-23-402 Ishibashi, Ikeda-shi, Osaka, JP) Tanaka, Shoji (4-9-1 Shiomi Cho, Ashiya-shi, Hyogo, JP) Matsuo, Hisayuki (5-15-141Onoharahigashi 5-Chome, Minoo shi, Osaka, JP) Mizuno, Kensaku (450 Ooaza Kihara Kiyotake-cho, Miyazaki-gun, Miyazaki, JP) BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, vol. 3, 30th June 1986, pages 984-991, Academic Press, Inc.; K. and precursor thereof produced by a recombinant DNA technique; a DNA coding for the enzyme or precursor thereof; a plasmid containing the DNA; a host organism transformed with the plasmid; a process for production of the enzyme using the transformant; and a process for production of a C-terminal α-amidated peptide using the enzyme. A process according to claim 2 wherein the prepro- C-terminal α-amidating enzyme has amino acid sequence (I) and wherein A represents the amino acid sequence (II) and B represents the amino acid sequence (III).7.A process according to claim 6 wherein the C-terminal α-amidating enzyme has amino acid sequence (IV) and wherein C represents the amino acid sequence (VI), X represents Ala, Y represents Thr, and Z represents Ala, and D represents the amino acid sequence (VII).8.

Miller MB, Yan Y, Machida K, Kiraly DD, Levy AD, Wu YI, Lam TT, Abbott T, Koleske AJ, Eipper BA, Mains RE.

MIZUNO et al.: "Peptide C- terminal alpha-amidating enzyme purified to homogeneity from Xenopus laevis skin" FEBS LETTERS, vol. 2, July 1986, pages 251-254, Elsevier Science Publishers B. MOLLAY et al.: "Detection and partial characterization of an amidating enzyme in skin secretion of Xenopus laevis" BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, vol.

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Kumar D, Blaby-Haas CE, Merchant SS, Mains RE, King SM, Eipper BA.

PMID: 27426256 Early eukaryotic origins for cilia-associated bioactive peptide-amidating activity. PMID: 26787743 60 YEARS OF POMC: From POMC and α-MSH to PAM, molecular oxygen, copper, and vitamin C.

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A process for production of a C-terminal α-amidated peptide or protein, characterized by reacting the enzyme according to claim 1 with a peptide or protein having a glycine residue at a C-terminal thereof. 3, 30th June 1986, pages 984-991, Academic Press, Inc.; K.

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