Serine hydroxymethyltransferase

Evidence for its presence in human, monkey and rat lenses

Arthur M. Geller, J. Samuel Zigler, Howard M. Jernigan

Research output: Contribution to journalArticle

Abstract

Serine hydroxymethyltransferase (SHMT) is present in cultured rat, monkey and human lenses as shown by 15N-serine or 15N-glycine labeling studies. Following incubation with 15N-serine, the percent enrichment of 15N in glycine increases with time, and vice versa, demonstrating the presence of the enzyme, and the reversibility of the reaction in intact cultured lenses. Similar patterns of 15N enrichment were found in all three species, but lenses from young rats showed a higher percent enrichment than lenses obtained from older animals. Label from 15N-serine or 15N-glycine was also incorporated into a number of other amino acids, including aspartate, alanine, glutamate and proline. Conclusive evidence for the presence of SHMT in rat lens homogenates has been obtained by direct enzyme assay. The specific activity of rat lens SHMT was age dependent; approximately 2·4 units per mg protein in day old rats, declining to about 0·15 units per mg in adult animals. The higher specific activity observed in younger animals is consistent with the 15N labeling results obtained with cultured lenses. Lens SHMT has been partially characterized. In the presence of excess tetrahydrofolate the assay was essentially linear with increasing time. With serine as the substrate, the enzyme requires tetrahydrofolate for activity, the pH optimum is between pH 7·5 and 8·3, the Km for serine is about 0·25 mm, and the enzyme is inhibited by cycloserine. In conclusion, this study demonstrates the existence of SHMT in rat, monkey and human lenses. Rat lens specific activity has been shown to decrease with increasing age, and the enzyme has been partially characterized. Activity was detected by measuring the direct formation of the product, N5,N10-methylenetetrahydrofolate, and by following the reversible interconversion of 15N-labeled serine and glycine in intact cultured lenses.

Original languageEnglish (US)
Pages (from-to)149-155
Number of pages7
JournalExperimental Eye Research
Volume50
Issue number2
DOIs
StatePublished - 1990
Externally publishedYes

Fingerprint

Glycine Hydroxymethyltransferase
Lenses
Haplorhini
Serine
Glycine
Enzymes
Cycloserine
Enzyme Assays
Proline
Aspartic Acid
Alanine
Glutamic Acid

Keywords

  • glycine
  • lens
  • methionine synthesis
  • serine
  • serine hydroxymethyltransferase
  • tetrahydrofolate
  • transaminase

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

Cite this

Serine hydroxymethyltransferase : Evidence for its presence in human, monkey and rat lenses. / Geller, Arthur M.; Zigler, J. Samuel; Jernigan, Howard M.

In: Experimental Eye Research, Vol. 50, No. 2, 1990, p. 149-155.

Research output: Contribution to journalArticle

Geller, Arthur M. ; Zigler, J. Samuel ; Jernigan, Howard M. / Serine hydroxymethyltransferase : Evidence for its presence in human, monkey and rat lenses. In: Experimental Eye Research. 1990 ; Vol. 50, No. 2. pp. 149-155.
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abstract = "Serine hydroxymethyltransferase (SHMT) is present in cultured rat, monkey and human lenses as shown by 15N-serine or 15N-glycine labeling studies. Following incubation with 15N-serine, the percent enrichment of 15N in glycine increases with time, and vice versa, demonstrating the presence of the enzyme, and the reversibility of the reaction in intact cultured lenses. Similar patterns of 15N enrichment were found in all three species, but lenses from young rats showed a higher percent enrichment than lenses obtained from older animals. Label from 15N-serine or 15N-glycine was also incorporated into a number of other amino acids, including aspartate, alanine, glutamate and proline. Conclusive evidence for the presence of SHMT in rat lens homogenates has been obtained by direct enzyme assay. The specific activity of rat lens SHMT was age dependent; approximately 2·4 units per mg protein in day old rats, declining to about 0·15 units per mg in adult animals. The higher specific activity observed in younger animals is consistent with the 15N labeling results obtained with cultured lenses. Lens SHMT has been partially characterized. In the presence of excess tetrahydrofolate the assay was essentially linear with increasing time. With serine as the substrate, the enzyme requires tetrahydrofolate for activity, the pH optimum is between pH 7·5 and 8·3, the Km for serine is about 0·25 mm, and the enzyme is inhibited by cycloserine. In conclusion, this study demonstrates the existence of SHMT in rat, monkey and human lenses. Rat lens specific activity has been shown to decrease with increasing age, and the enzyme has been partially characterized. Activity was detected by measuring the direct formation of the product, N5,N10-methylenetetrahydrofolate, and by following the reversible interconversion of 15N-labeled serine and glycine in intact cultured lenses.",
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