BCH210H1 Lecture Notes - Lecture 19: Zymogen, Spectrophotometry, Phosphatase

• School: UTSG
• Department: Biochemistry
• Course: BCH210H1
• Professor: Reinhart Reithmeier

Document Summary

Modifications: substrate availability, covalent modifications, allosteric control, zymogen, proenzymes. Don"t make substrate nothing for enzyme to catalyze: stop cell"s production of substrate. Event of stroke / heart attack production of phospholipase a2 (pla2) Pla2 cleaves off c2 fatty acid creates arachidonic acid. Arachidonic acid + o2 w/ cox (cyclooxygenase) eicosanoids: eicosanoids: trigger prostaglandins, leukotrienes, and. Thromboxane release: normally arachidonic acid (substrate) concentration is not high in body, not available. Major mechanism: phosphorylation: onto -oh functional residues, serine & threonine residues, reversible, w/ kinases. Phosphatase: removes p group in h2o presence. Phophorylase kinase phosphorylates phosphorylase b & turns it on (into phosphorylase a: phosphorylating can have different effects depending on target molecules. Phosphorylase a takes off glucose & adds pi: phosphorylysis: adds an inorganic phosphate. Allosteric site binds modulator: induces conformational change. Regulatory subunits (in multiple-subunit enzymes: binds modulators, induces change in the catalytic subunit. Threonine e1 e2 e3 e4 e5 isoleucine.