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. 1974 Oct;120(1):168–172. doi: 10.1128/jb.120.1.168-172.1974

Purification and Properties of 4-Hydroxy-2-Ketopimelate Aldolase from Acinetobacter

Pak-Tong Leung 1, Peter J Chapman 1, Stanley Dagley 1
PMCID: PMC245746  PMID: 4429638

Abstract

The chemical synthesis of 4-hydroxy-2-ketopimelic acid is described. An aldolase that cleaves this compound to succinic semialdehyde and pyruvate has been purified from Acinetobacter grown at the expense of 4-hydroxyphenylacetic acid. The molecular weight of the enzyme was about 158,000 from sedimentation equilibrium data; other physical determinations gave values in reasonable agreement. The protein was globular and was dissociated in sodium dodecyl sulfate to give a species of molecular weight 25,700. The enzyme attacked both enantiomers of synthetic 4-hydroxy-2-ketopimelate and was stimulated by Mg2+ and Mn2+ ions.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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