The Lighter Side Song: Catalyze (To the Tune of ‘‘Close to You’’)y h S Received for publication, March 9, 2010 Kevin Ahern‡ From the Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331 My enzymes Truly are inclined To convert Things they bind Turn the key Covalently Cat-a-lyze How do cells Regulate these roles? Allo-ster -ic controls Two forms, see States R and T Mod-u-late Competing inhibition keeps The substrates from the active site They raise Km, but leave Vmax and shirk While the non-competers bind elsewhere And lift the plot made on Lineweaver-Burk * Other ways Enzymes can be blocked When things bind Then get locked Stuck not free Tied to the key Su-i-cide Penicillin’s action stops Peptidoglycan cross-links in Bacterial cell walls in awesome ways Beta lactam ring’s reactive site Starts bonding with D-D-transpeptidase So there are Several enzyme states Counteract -ing substrates Now you see Blocking the key Regulates Cat-a-lysts Have to be controlled Some get slowed Put on hold It’s sublime How the enzymes (slow) Cat-a-lyze ahhhhhhhhhhhhhhhhhhh - cat-a-lyze ahhhhhhhhhhhhhhhhhhh - cat-a-lyze ahhhhhhhhhhhhhhhhhhh - cat-a-lyze h S Additional Supporting Information (a .mp3 ﬁle of this song) may be found in the online version of this article. *Km and Vmax may each be changed by inhibition mecha- nisms †Copyright @ 2009 Kevin Ahern ‡To whom correspondence should be addressed. Tel.: 541-737-2305. E-mail: [email protected]. This paper is available on line at http://www.bambed.org DOI 10.1002/bmb.20412 355 Q 2010 by The International Union of Biochemistry and Molecular Biology BIOCHEMISTRY AND MOLECULAR BIOLOGY EDUCATION Vol. 38, No. 5, pp. 355, 2010

Song: Catalyze (to the tune of “Close to You”)

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Page 1: Song: Catalyze (to the tune of “Close to You”)

The Lighter Side

Song: Catalyze (To the Tune of ‘‘Close to You’’)yhSReceived for publication, March 9, 2010

Kevin Ahern‡

From the Department of Biochemistry and Biophysics, Oregon State University, Corvallis, Oregon 97331

My enzymesTruly are inclinedTo convertThings they bindTurn the keyCovalentlyCat-a-lyze

How do cellsRegulate these roles?Allo-ster-ic controlsTwo forms, seeStates R and TMod-u-late

Competing inhibition keepsThe substrates from the active siteThey raise Km, but leave Vmax and shirkWhile the non-competers bind elsewhereAnd lift the plot made on Lineweaver-Burk*

Other waysEnzymes can be blockedWhen things bindThen get lockedStuck not freeTied to the keySu-i-cide

Penicillin’s action stopsPeptidoglycan cross-links inBacterial cell walls in awesome waysBeta lactam ring’s reactive siteStarts bonding with D-D-transpeptidase

So there areSeveral enzyme statesCounteract-ing substratesNow you seeBlocking the keyRegulates

Cat-a-lystsHave to be controlledSome get slowedPut on holdIt’s sublimeHow the enzymes(slow) Cat-a-lyze

ahhhhhhhhhhhhhhhhhhh - cat-a-lyzeahhhhhhhhhhhhhhhhhhh - cat-a-lyzeahhhhhhhhhhhhhhhhhhh - cat-a-lyze

hS Additional Supporting Information (a .mp3 file of this song)may be found in the online version of this article.

*Km and Vmax may each be changed by inhibition mecha-nisms

†Copyright @ 2009 Kevin Ahern‡To whom correspondence should be addressed. Tel.:

541-737-2305. E-mail: [email protected].

This paper is available on line at http://www.bambed.org DOI 10.1002/bmb.20412355

Q 2010 by The International Union of Biochemistry and Molecular Biology BIOCHEMISTRY AND MOLECULAR BIOLOGY EDUCATION

Vol. 38, No. 5, pp. 355, 2010