GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

PMID:4972917

From GONUTS
Jump to: navigation, search
Citation

Grandgenett, DP and Stahly, DP (1968) Diaminopimelate decarboxylase of sporulating bacteria. J. Bacteriol. 96:2099-109

Abstract

The meso-diaminopimelate (DAP) decarboxylase of Bacillus licheniformis, a pyridoxal phosphate-requiring enzyme, was stabilized in vitro by 0.15 m sodium phosphate buffer (pH 7.0) containing 1 mm 2,3-dimercaptopropan-1-ol, 100 mug of pyridoxal phosphate per ml, and 3 mm DAP. When the meso-DAP concentration was varied, the enzyme in cell-free extracts of B. licheniformis exhibited Michaelis-Menten kinetics. Pyridoxal phosphate was the only pyridoxine derivative which acted as a cofactor. The enzyme was subject to both inhibition and repression by l-lysine. The inhibitory effect of lysine was on the K(m) (meso-DAP). A maximum repression of about 20% was obtained. No significant inhibition or activation was produced by cadaverine, dipicolinic acid, phenylalanine, pyruvate, ethylenediamine-tetraacetate, adenosine triphosphate, adenosine diphosphate, or adenosine monophosphate. When B. licheniformis was grown in an ammonium lactate-glucose-salts medium, an increase in DAP decarboxylase specific activity occurred during cellular growth with a maximal specific activity at the end of the exponential phase. As soon as growth ceased, the specific activity of the enzyme decreased to approximately one-half of the maximal specific activity and remained at this level thereafter. When B. cereus was grown in complex media, there was an increase in DAP decarboxylase specific activity up to the end of the exponential phase. Thereafter, the specific activity decreased to a nondetectable level in 4 hr. Dipicolinic acid synthesis was first detected 15 min later and was essentially complete after an additional 2.5 hr. The significance of the disappearance of DAP decarboxylase in B. cereus was discussed with regard to control of dipicolinic acid and spore mucopeptide biosynthesis.

Links

PubMed PMC252563

Keywords

Bacillus/enzymology; Bacillus/growth & development; Bacillus/metabolism; Bacillus cereus/enzymology; Carboxy-Lyases; Chromatography, Paper; Dimercaprol/metabolism; Enzyme Repression; Lysine/biosynthesis; Lysine/pharmacology; Penicillamine/pharmacology; Picolinic Acids/biosynthesis; Pimelic Acids/analysis; Pimelic Acids/metabolism; Pyridoxal Phosphate/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

BACLD:Q65HV3

GO:0008836 : diaminopimelate decarboxylase activity

ECO:0000314:

F

figure 2 shows that Meso-DAP conversion to L-lysine was demonstrated by paperchromatography

complete
CACAO 4395

BACLD:Q65HV3

enables

GO:0008836: diaminopimelate decarboxylase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete


See also

References

See Help:References for how to manage references in GONUTS.