why alcohol dehydrogenase catalyze ethanol better than anyother alcohol?

simple the substrate for the enzyme ADH is ethanol and not phenol.  Phenol has different properties for one it is acidic (one of the only alcohols that is) and has a big old benzene ring coming off it making it physically hard to get the alcohol part into the enzyme.  Ethanol is small and can fit into the enzyme correctly.  The old lock and key terminology i think works best to describe the relationship between the enzyme and the substrate.  
When you make drugs that are going to act on a certain enzyme you create similar structures with something tweaked to prevent the enzyme from using the drug correctly resulting in it being occupied by the drug preventing the natural substrate from getting to the enzyme.

Lastly there are terms called affinity and intrinsic activity.  compounds tha react quickly and a well with an enzyme (like etOH to ADH) are said to have high intrinsic activity.  Affinity is essentially how well a compound fits into an enzyme, the higher the affinity the better the compound fits into the enzyme.  So in essence etOH has high affinity and high intrinsic activity with ADH.  Whereas other alcohols (propanol-lacks affinity to ADH, probably will react well with ADH but the extra carbon prevents it from fitting in there well.  Phenol-lacks both affinity and intrinsic activity, the big benzene ring prevents it from fitting in the enzyme (low affinity) and fact that the alcohol is now acidic it lacks intrinsic activity with the enzyme.  making it a very poor choice.
All this talk is making me crave a beer.  adios.