Peptide amidation

Production of peptide hormones in vivo and in vitro

Kyun Hwan Kim, Baik Lin Seong

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Over half of all biologically active peptides and peptide hormones are α-amidated at their C-terminus, which is essential for their full biological activities. Amidation is accomplished through the sequential reaction of the two enzymes encoded by the single bifunctional, peptidylglycine α-amidating monooxygenase (PAM or an α-amidating enzyme). PAM catalyzes the formation of a peptide amide from peptide precursors that include a C-terminal glycine, and requires copper, molecular oxygen, and ascorbate. PAM is the only enzyme that produces peptide amides in vivo. However, various strategies utilizing PAM, carboxypeptidase-Y enzymes, and chemical synthesis have been developed for producing peptide amides in vitro. The growing need and importance of peptide amide drugs has highlighted the necessity for an efficient in vitro amidating system for industrial application. In recent years, recombinant systems for enzymatic amidation have received growing attention for the production of peptide hormones, like calcitonin and oxytocin. This review presents the current situation regarding amidation, with a special emphasis on the industrial production of peptide hormones.

Original languageEnglish
Pages (from-to)244-251
Number of pages8
JournalBiotechnology and Bioprocess Engineering
Volume6
Issue number4
DOIs
Publication statusPublished - 2001 Jan 1

Fingerprint

Peptide Hormones
Peptides
Pulse amplitude modulation
Amides
Enzymes
Cathepsin A
Molecular oxygen
Calcitonin
Oxytocin
Mixed Function Oxygenases
Bioactivity
Glycine
Industrial applications
In Vitro Techniques
Amino acids
Copper
Oxygen
Pharmaceutical Preparations

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology
  • Biomedical Engineering

Cite this

@article{550844a023f74a188db51c924e98c510,
title = "Peptide amidation: Production of peptide hormones in vivo and in vitro",
abstract = "Over half of all biologically active peptides and peptide hormones are α-amidated at their C-terminus, which is essential for their full biological activities. Amidation is accomplished through the sequential reaction of the two enzymes encoded by the single bifunctional, peptidylglycine α-amidating monooxygenase (PAM or an α-amidating enzyme). PAM catalyzes the formation of a peptide amide from peptide precursors that include a C-terminal glycine, and requires copper, molecular oxygen, and ascorbate. PAM is the only enzyme that produces peptide amides in vivo. However, various strategies utilizing PAM, carboxypeptidase-Y enzymes, and chemical synthesis have been developed for producing peptide amides in vitro. The growing need and importance of peptide amide drugs has highlighted the necessity for an efficient in vitro amidating system for industrial application. In recent years, recombinant systems for enzymatic amidation have received growing attention for the production of peptide hormones, like calcitonin and oxytocin. This review presents the current situation regarding amidation, with a special emphasis on the industrial production of peptide hormones.",
author = "Kim, {Kyun Hwan} and Seong, {Baik Lin}",
year = "2001",
month = "1",
day = "1",
doi = "10.1007/BF02931985",
language = "English",
volume = "6",
pages = "244--251",
journal = "Biotechnology and Bioprocess Engineering",
issn = "1226-8372",
publisher = "Korean Society for Biotechnology and Bioengineering",
number = "4",

}

Peptide amidation : Production of peptide hormones in vivo and in vitro. / Kim, Kyun Hwan; Seong, Baik Lin.

In: Biotechnology and Bioprocess Engineering, Vol. 6, No. 4, 01.01.2001, p. 244-251.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Peptide amidation

T2 - Production of peptide hormones in vivo and in vitro

AU - Kim, Kyun Hwan

AU - Seong, Baik Lin

PY - 2001/1/1

Y1 - 2001/1/1

N2 - Over half of all biologically active peptides and peptide hormones are α-amidated at their C-terminus, which is essential for their full biological activities. Amidation is accomplished through the sequential reaction of the two enzymes encoded by the single bifunctional, peptidylglycine α-amidating monooxygenase (PAM or an α-amidating enzyme). PAM catalyzes the formation of a peptide amide from peptide precursors that include a C-terminal glycine, and requires copper, molecular oxygen, and ascorbate. PAM is the only enzyme that produces peptide amides in vivo. However, various strategies utilizing PAM, carboxypeptidase-Y enzymes, and chemical synthesis have been developed for producing peptide amides in vitro. The growing need and importance of peptide amide drugs has highlighted the necessity for an efficient in vitro amidating system for industrial application. In recent years, recombinant systems for enzymatic amidation have received growing attention for the production of peptide hormones, like calcitonin and oxytocin. This review presents the current situation regarding amidation, with a special emphasis on the industrial production of peptide hormones.

AB - Over half of all biologically active peptides and peptide hormones are α-amidated at their C-terminus, which is essential for their full biological activities. Amidation is accomplished through the sequential reaction of the two enzymes encoded by the single bifunctional, peptidylglycine α-amidating monooxygenase (PAM or an α-amidating enzyme). PAM catalyzes the formation of a peptide amide from peptide precursors that include a C-terminal glycine, and requires copper, molecular oxygen, and ascorbate. PAM is the only enzyme that produces peptide amides in vivo. However, various strategies utilizing PAM, carboxypeptidase-Y enzymes, and chemical synthesis have been developed for producing peptide amides in vitro. The growing need and importance of peptide amide drugs has highlighted the necessity for an efficient in vitro amidating system for industrial application. In recent years, recombinant systems for enzymatic amidation have received growing attention for the production of peptide hormones, like calcitonin and oxytocin. This review presents the current situation regarding amidation, with a special emphasis on the industrial production of peptide hormones.

UR - http://www.scopus.com/inward/record.url?scp=4544386057&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=4544386057&partnerID=8YFLogxK

U2 - 10.1007/BF02931985

DO - 10.1007/BF02931985

M3 - Article

VL - 6

SP - 244

EP - 251

JO - Biotechnology and Bioprocess Engineering

JF - Biotechnology and Bioprocess Engineering

SN - 1226-8372

IS - 4

ER -