A model for the regulation of D-3-phosphoglycerate dehydrogenase, a Vmax-type allosteric enzyme

Protein Science

Volumn 5, Issue 1, 1996, Pages 34-41

  Grant, Gregory A ^a   Schuller, David J ^b   Banaszak, Leonard J ^c  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF MINNESOTA   (United States)

Author keywords

Enzyme control; Multidomain enzyme; Phosphoglycerate dehydrogenase; Velocity modulated allosterism

Indexed keywords

BACTERIAL ENZYME; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;

ARTICLE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME KINETICS; ENZYME REGULATION; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN;

ALLOSTERIC REGULATION; CARBOHYDRATE DEHYDROGENASES; ESCHERICHIA COLI; HYDROGEN BONDING; KINETICS; MODELS, CHEMICAL; PHOSPHOGLYCERATE DEHYDROGENASE; PROTEIN CONFORMATION; SERINE; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0029670622     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560050105     Document Type: Article

References (17)

1. Dubrou RD, Pizer LI. 1977a. Transient kinetic studies on the allosteric transition of phosphoglycerate dehydrogenase. J Biol Chem 252:1527-1538.
2. Dubrow RD, Pizer LI. 1977b. Transient kinetic and deuterium isotope effects studies on the catalytic mechanism of phosphoglycerate dehydrogenase. J Biol Chem 252:1539-1551.
3. Ferrin T, Huang C, Jarvis L, Langridge R. 1988. The MIDAS display system. J Mol Graphics 6:13-27.
4. Goldberg JD, Yoshida T, Brick P 1994. Crystal structure of an NAD-dependent D-glycerate dehydrogenase at 2.4 À resolution. J Mol Biol 236:1123-1140.
5. Grant GA. 1989. A new family of 2-hydroxy acid dehydrogenases. Biochem Biophys Res Commun 165:1371-1374.
6. Grant GA, Zapp ML 1981. D-3-Phosphoglycerate dehydrogenase from Escherichia coli. Isolation by affinity chromatography and sequence comparison to other dehydrogenases. Biosci Rep 1:733-741.
7. glc with glycerol kinase. Science 259:673-677.
8. Lamzin VS, Dauter Z, Popov VO, Harutyunyun EH, Wilson K. 1994. High resolution structures of holo and apo formate dehydrogenase. J Mol Biol 236:759-785.
9. Monod J, Wyman J, Changeux JP. 1965. On the nature of allosteric transitions: A plausible model. J Mol Biol 12:88-118.
10. Pizer LI. 1963. The pathway and control of serine biosynthesis in Escherichia coli. J Biol Chem 238:3934-3944.
11. Rosenbloom J, Sugimoto E, Pizer LI. 1968. The mechanism of end product inhibition of serine biosynthesis: III. Physical and chemical properties of phosphoglycerate dehydrogenase. J Biol Chem 243:2099-2107.
12. max-type cooperative enzyme: D-3-phosphoglycerate dehydrogenase. Nature Struct Biol 2:69-76.
13. Schuller DJ, Fetter CH, Banaszak LJ, Grant GA. 1989. Enhanced expression of the Escherichia coli serA gene in a plasmid vector. J Biol Chem 264:2645-2648.
14. Sugimoto E, Pizer LI. 1968a. The mechanism of end product inhibition of serine biosynthesis: I. Purification and kinetics of phosphoglycerate dehydrogenase. J Biol Chem 243:2081-2089.
15. Sugimoto E, Pizer LI 1968b. The mechanism of end product inhibition of serine biosynthesis: II. Optical studies of phosphoglycerate dehydrogenase. J Biol Chem 243:2090-2098.
16. Tobey KL, Grant GA. 1986. The nucleotide sequence of the serA gene of Escherichia coli and the amino acid sequence of the encoded protein, D-3-phosphoglycerate dehydrogenase. J Biol Chem 261:12179-12183.
17. Winicow I, Pizer LI. 1974. The mechanism of end product inhibition of serine biosynthesis: IV. Subunit structure of phosphoglycerate dehydrogenase and steady state kinetic studies of phosphoglycerate oxidation. J Biol Chem 249:1348-1355.