Daff, Simon; Manson, Forbes D. C.; Reid, Graeme A.; Chapman, Stephen K. published the artcile< Strategic manipulation of the substrate specificity of Saccharomyces cerevisiae flavocytochrome b2>, Name: (9Z,12Z)-Methyl octadeca-9,12-dienoate, the main research area is cytochrome b5 lactate dehydrogenase substrate specificity; Saccharomyces cytochrome b5 lactate dehydrogenase specificity.
Flavocytochrome b2 from Saccharomyces cerevisiae acts physiol. as an L-lactate dehydrogenase. Although L-lactate is its primary substrate, the enzyme is also able to utilize a variety of other (S)-2-hydroxy acids. Structural studies and sequence comparisons with several related flavoenzymes have identified the key active-site residues required for catalysis. However, the residues Ala-198 and Leu-230, found in the X-ray-crystal structure to be in contact with the substrate Me group, are not well conserved. The authors propose that the interaction between these residues and a prospective substrate mol. has a significant effect on the substrate specificity of the enzyme. In an attempt to modify the specificity in favor of larger substrates, three mutant enzymes have been produced: A198G, L230A and the double mutant A198G/L230A. As a means of quantifying the overall kinetic effect of a mutation, substrate-specificity profiles were produced from steady-state experiments with (S)-2-hydroxy acids of increasing chain length, through which the catalytic efficiency of each mutant enzyme with each substrate could be compared with the corresponding wild-type efficiency. The Ala-198 → Gly mutation had little influence on substrate specificity and caused a general decrease in enzyme efficiency. However, the Leu-230 → Ala mutation caused the selectivity for 2-hydroxyoctanoate over lactate to increase by a factor of 80.
Biochemical Journal published new progress about Enzyme kinetics. 112-63-0 belongs to class esters-buliding-blocks, and the molecular formula is C19H34O2, Name: (9Z,12Z)-Methyl octadeca-9,12-dienoate.
Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics