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The severely acclaimed laboratory general, Methods in Enzymology, is among the such a lot hugely revered courses within the box of biochemistry. when you consider that 1955, every one quantity has been eagerly awaited, usually consulted, and praised via researchers and reviewers alike. The sequence comprises a lot fabric nonetheless correct at the present time - really an important booklet for researchers in all fields of lifestyles sciences

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Extra info for Enzyme Kinetics and Mechanism - Part C: Intermediates, Stereochemistry, and Rate Studies

Example text

Sample data for the forward direction are presented in Fig. 2. The plots fit Eq. (2), which is the rate law corresponding to the 1 v - 1 V + KUDPGlc V[UDPGlc] KGaI-I_ P + (2) V[GaI-1-P] Ping Pong Bi Bi kinetic model of Eqs. UDPGal ~ E-XH + UDPGal (4) Product inhibition patterns fully support the assignment of the Ping Pong Bi Bi kinetic model. According to Cleland's rules applied to Eqs. 4 02 0 I 5 10 15 20 [6aJact0se I phosphate]-~ mM-' 25 Flo. 2. Double reciprocal plots of initial velocities of glucose I-P formation at varying [galactose l-P] and several fixed [UDPglucose].

The velocity units are the same as those in Fig. 3. 1 1 ( Kuo~a I KUDr~al[UDPGIc] ~ v =-~ _ 1 + [UDPGal] + ~ ] . + KGIv1-P + KuDr~a~KiGlc_I_v[UDPGIc]~ ~ 1 7 [Glc-l-P] (6) All o f the o t h e r p r o d u c t inhibitions predicted b y this p a t h w a y h a v e also b e e n verified. 7 A n o t h e r kinetic p r o p e r t y characteristic o f the Ping P o n g Bi Bi pathw a y is inhibition by high levels o f substrates. This results f r o m substrates binding to the w r o n g e n z y m e f o r m s , in the p r e s e n t case the uridylyl d o n o r substrates binding to u r i d y l y l - X - E and the a c c e p t o r substrates binding to E - X H .

7,s Enzyme containing covalently bound azp was isolated by gel filtration after incubating phosphoglycerate mutase briefly with glycerate-2, 3-P2-[U-32p]. At least 90% of the protein-bound phosphoryl group was released as orthophosphate upon acidification (Fig. 2). This indicates that the phosphate is not associated with the enzyme in the form of glycerate-2-P, glycerate-3-P, or glycerate2,3-P2. Upon phenol extraction (see Methods), the radioactivity remained associated with the protein in the phenol layer.

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