Comparison of a carboxypeptidase E-like enzyme in human, bovine, mouse, Xenopus, shark and Aplysia neural tissue

Lloyd D. Fricker, Edward Herbert

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Several diverse species contain an enzyme with many properties in common with those of bovine carboxypeptidase E (CPE), a neuropeptide processing carboxypeptidase B-like enzyme. This enzyme has been designated EC 3.4.17.10, and is also known as enkephalin convertase and carboxypeptidase H. All tissues that are known to contain bioactive peptides also contain CPE-like enzymatic activity. In Xenopus laevis, enzyme activity is highest in the brain and pituitary, lower in the skin, and undetectable in liver and gut. In Aplysia californica, enzyme activity is highest in the atrial gland, but is also present in moderate amounts in the various neural tissue. CPE extracted from human, bovine, mouse, Xenopus, shark, and Aplysia neural tissue is substantially purified using substrate affinity chromatography and concanavalin A sepharose columns. The partially purified enzyme from all species examined possess very similar enzymatic properties. These properties include a pH optimum of 5.6, a stimulation by cobalt chloride, and an inhibition by chelating agents (1,10-phenanthroline). Arginine-derived active site-directed inhibitors show similar inhibition constants (Ki'ms) towards enzyme from the various species, whereas lysine-derived inhibitors are substantially less potent towards the Aplysia carboxypeptidase than towards enzyme isolated from the other species. The similar properties of the carboxypeptidase isolated from the various species suggests that a CPE-like is involved in the biosynthesis of many peptide neurotransmitters and hormones in a wide range of organisms.

Original languageEnglish (US)
Pages (from-to)281-286
Number of pages6
JournalBrain Research
Volume453
Issue number1-2
DOIs
StatePublished - Jun 21 1988
Externally publishedYes

Fingerprint

Carboxypeptidase H
Sharks
Aplysia
Xenopus
Enzymes
Carboxypeptidases
Carboxypeptidase B
Peptide Hormones
Xenopus laevis
Chelating Agents
Neuropeptides
Affinity Chromatography
Lysine
Neurotransmitter Agents
Arginine
Catalytic Domain

Keywords

  • Carboxypeptidase B-like
  • Carboxypeptidase H
  • Enkephalin convertase
  • Neuropeptide biosynthesis
  • Processing enzyme

ASJC Scopus subject areas

  • Developmental Biology
  • Molecular Biology
  • Clinical Neurology
  • Neuroscience(all)

Cite this

Comparison of a carboxypeptidase E-like enzyme in human, bovine, mouse, Xenopus, shark and Aplysia neural tissue. / Fricker, Lloyd D.; Herbert, Edward.

In: Brain Research, Vol. 453, No. 1-2, 21.06.1988, p. 281-286.

Research output: Contribution to journalArticle

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