The hydratase activity of malonate semialdehyde decarboxylase: Mechanistic and evolutionary implications

Journal of the American Chemical Society

Volumn 126, Issue 48, 2004, Pages 15658-15659

  Poelarends, Gerrit J ^a   Serrano, Hector ^a   Johnson Jr , William H ^a   Hoffman, David W ^a   Whitman, Christian P ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLYASE; HYDROLYASE; MALONATE SEMIALDEHYDE DECARBOXYLASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; DECARBOXYLATION; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MECHANISM; HYDRATION; IONIZATION; MEASUREMENT; MICHAEL ADDITION; MOLECULE; PH; PROTEIN FAMILY; PROTON NUCLEAR MAGNETIC RESONANCE; REACTION ANALYSIS; SEQUENCE ANALYSIS;

EID: 10044221852     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja044304n     Document Type: Article

References (25)

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11. 4 buffer (1 mL, pH 9.0), and assayed for residual MSAD activity. No significant loss of activity was observed.
12. 4b A similar reaction mixture without MSAD, incubated for 16 h, showed no spectral evidence for 6 or derivatives. In aqueous solution, 6 is in equilibrium with the hydrate and the enol: Guthrie, J. P. J. Am. Chem. Soc. 1972, 94, 7020-7024.
13. Although ∼39% of the enzyme exists with Pro-1 in the neutral state at pH 9.0. enzyme inactivation is not observed under the experimental conditions.
14. 4 buffer, pH 9.0. The pH of the stock solutions was adjusted to about 8.5. The concentrations of 4 used in the kinetic assay ranged from 0.05 to 12 mM.
15. 1
16. The MSAD mutants were prepared as described1.
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24. Almrud, J. J.; Poelarends, G. J.; Serrano, H.; Johnson, W. H., Jr.; Hackert, M. L.; Whitman, C. P. 2004, unpublished results.
25. 4a The presence of a contaminating protein is unlikely but cannot be excluded. Nonenzymatic decay of 2 prevents a determination of whether CaaD has low-level MSAD activity.