Subcellular distribution of enzymes of transmethylation and transsulphuration in rat brain

D. K. Rassin, G. E. Gaull

Research output: Contribution to journalArticle

66 Citations (Scopus)

Abstract

Certain of the sulphur containing amino acids have been associated with synaptic transmission of the central nervous system. The enzymes involved in the synthesis of these putative neurotransmitter or modulator compounds have a different subcellular distribution in rat brain from those enzymes that catalyse the synthesis of other compounds in this pathway. Methionine adenosyltransferase and 5 methyl tetrahydrofolate homocysteine methyltransferase catalyse reactions that maintain the methylation functions of the pathway and are found in soluble fractions. Cystathionine β synthase, cystathionase, cysteine dioxygenase and cysteine sulphinic acid decarboxylase catalyse the synthesis of those sulphur containing amino acids implicated in neurotransmitter functions and these enzymes have both particulate and soluble components. Serine hydroxymethyltransferase, which also has a particulate fraction in brain, is responsible for the synthesis of the neurotransmitter glycine, in addition to its role in the methionine related metabolism of folate.

Original languageEnglish (US)
Pages (from-to)969-978
Number of pages10
JournalJournal of Neurochemistry
Volume24
Issue number5
StatePublished - 1975
Externally publishedYes

Fingerprint

Sulfur Amino Acids
Neurotransmitter Agents
Rats
Brain
sulfoalanine decarboxylase
Homocysteine S-Methyltransferase
Cysteine Dioxygenase
Enzymes
Methionine Adenosyltransferase
Glycine Hydroxymethyltransferase
Cystathionine gamma-Lyase
Sulfur
Cystathionine
Folic Acid
Amino Acids
Synaptic Transmission
Methionine
Glycine
Methylation
Neurology

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Subcellular distribution of enzymes of transmethylation and transsulphuration in rat brain. / Rassin, D. K.; Gaull, G. E.

In: Journal of Neurochemistry, Vol. 24, No. 5, 1975, p. 969-978.

Research output: Contribution to journalArticle

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