The 80s loop of the catalytic chain of Escherichia coli aspartate transcarbamoylase is critical for catalysis and homotropic cooperativity

Protein Science

Volumn 8, Issue 6, 1999, Pages 1305-1313

  Macol, Christine ^a   Dutta, Malini ^a   Stec, Boguslaw ^a   Tsuruta, Hiro ^b   Kantrowitz, Evan R ^a  

^a BOSTON COLLEGE   (United States)

^b SLAC NATIONAL ACCELERATOR LABORATORY   (United States)

Author keywords

Allosteric enzyme; Complementation; Low angle X ray scattering; Molecular dynamics

Indexed keywords

ASPARTATE CARBAMOYLTRANSFERASE;

ARTICLE; CATALYSIS; ENZYME ACTIVE SITE; ESCHERICHIA COLI; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; STEREOCHEMISTRY; X RAY ANALYSIS;

EID: 0032992238     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.6.1305     Document Type: Article

References (51)

1. Baker DP, Kantrowitz ER. 1993. The conserved residues glutamate-37, asparate-100 and arginine-269 are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase. Biochemistry 32:10150-10158.
2. Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
3. Collins KD, Stark GR. 1969. Aspartate transcarbamylase: Studies of the catalytic subunit by ultraviolet difference spectroscopy. J Biol Chem 244:1869-1877.
4. Collins KD, Stark GR. 1971. Aspartate transcarbamylase: Interaction with the transition state analogue N-(phosphonacetyl)-L-aspartate. J Biol Chem 246:6599-6605.
5. Fetler L, Taue P, Hervé G, Moody MF, Vachette P. 1995. X-ray scattering titration of the quaternary structure transition of aspartate transcarbamylase with a bisubstrate analogue: Influence of nucleotide effectors. J Mol Biol 251:243-255.
6. Gerhart JC. 1970. A discussion of the regulatory properties of aspartate transcarbamylase from Escherichia coli. Curr Top Cell Regul 2:275-325.
7. Gerhart JC, Pardee AB. 1962. Enzymology of control by feedback inhibition. J Biol Chem 237:891-896.
8. Gouaux JE, Krause KL, Lipscomb WN. 1987. The catalytic mechanism of Escherichia coli aspartate carbamoyltransferase: A molecular modeling study. Biochem Biophys Res Commun 142:893-897.
9. Gouaux JE, Lipscomb WN. 1988. Three-dimensional structure of carbamyl phosphate and succinate bound to aspartate carbamyltransferase. Proc Natl Acad Sci USA 85:4205-4208.
10. Gouaux JE, Lipscomb WN. 1990. Crystal structures of phosphonoacetamide ligated T and phosphonoacetamide and malonate ligated R states of aspartate carbamoyltransferase at 2.8 Å resolution and neutral pH. Biochemistry 29:389-402.
11. Greenwell P, Jewett SL, Stark GR. 1973. Aspartate transcarbamylase from Escherichia coli: The use of pyridoxal 5′-phosphate as a probe in the active site. J Biol Chem 248:5994-6001.
12. Griffin JH, Rosenbusch JP, Weber KK, Blout ER. 1972. Conformational changes in aspartate transcarbamylase. 1. Studies of ligand binding and of subunit interactions by circular dichroism spectroscopy. J Biol Chem 247:6482-6490.
13. Hervé G, Moody MF, Tauc P, Vachette P, Jones PT. 1985. Quaternary structure changes in aspartate transcarbamylase studied by X-ray solution scattering; Signal transmission following effector binding. J Mol Biol 185:189-199.
14. Hsuanyu Y, Wedler FC. 1987. Kinetic mechanism of native Escherichia coli aspartate transcarbamylase. Arch Biochem Biophys 259:316-330.
15. Jacobson GR, Stark GR. 1973. Aspartate transcarbamylases. Enzymes (3rd ed.) 9:225-308.
16. Kantrowitz ER, Lipscomb WN. 1977. Functionally important arginine residues of aspartate transcarbamylase. J Biol Chem 252:2873-2880.
17. Kantrowitz ER, Lipscomb WN. 1990. Escherichia coli aspartate transcarbamoylase: The molecular basis for a concerted allosteric transition. Trends Biochem Sci (Pers Ed) 15:53-59.
18. Kempe TD, Stark GR. 1975. Pyridoxal 5′-phosphate, a fluorescent probe in the active site of aspartate transcarbamoylase. J Biol Chem 250:6861-6869.
19. Kerbiriou D, Hervé G. 1972. Biosynthesis of an aspartate transcarbamylase lacking co-operative interactions. I. Disconnection of homotropic and heterotropic interactions under the influence of 2-thiouracil. J Mol Biol 64:379-392.
20. Krause KL, Voltz KW, Lipscomb WN. 1985. Structure at 2.9-Å resolution of aspartate carbamoyltransferase complexed with the bisubstrate analogue N-(phosphonacetyl)-L-aspartate. Proc Natl Acad Sci USA 82:1643-1647.
21. Krause KL, Voltz KW, Lipscomb WN. 1987. 2.5 Å structure of aspartate carbamoyltransferase complexed with the bisubstrate analog N-(phosphonacetyl)-L-aspartate. J Mol Biol 193:527-553.
22. Kunkel TA. 1985. Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc Natl Acad Sci USA 82:488-492.
23. Kunkel TA, Roberts JD, Zakour RA. 1987. Rapid and efficient site-specific mutagenesis without phenotype selection. Methods Enzymol 154:367-382.
24. Ladjimi MM, Middleton SA, Kelleher KS, Kantrowitz ER. 1988. Relationship between domain closure and binding, catalysis, and regulation in Escherichia coli aspartate transcarbamylase. Biochemistry 27:268-276.
25. Lahue RS, Schachman HK. 1984. The influence of quaternary structure of the active site of an oligomeric enzyme. Catalytic subunit of aspartate transcarbamoylase. J Biol Chem 259:13906-13913.
26. Landfear SM, Evans DR, Lipscomb WN. 1978a. Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue. Proc Natl Acad Sci USA 75:2654-2658.
27. Landfear SM, Lipscomb WN, Evans DR. 1978b. Functional modifications of aspartate transcarbamylase induced by nitration with tetranitromethane. J Biol Chem 253:3988-3996.
28. Lauritzen AM, Lipscomb WN. 1982. Modification of three active site lysine residues in the catalytic subunit of aspartate transcarbamylase by D-and L-bromosuccinate. J Biol Chem 257:1312-1319.
29. Lipscomb WN. 1994. Aspartate transcarbamoylase from Escherichia coli: Activity and regulation. Adv Enzymol 68:67-151.
30. Middleton SA, Kantrowitz ER. 1988. The function of Arg-234 and Asp-271 in domain closure, cooperativity and catalysis in Escherichia coli aspartate transcarbamylase. Biochemistry 27:8653-8660.
31. Middleton SA, Stebbins JW, Kantrowitz ER. 1989. A loop involving catalytic chain residues 230-245 is essential for the stabilization of both allosteric forms of Escherichia coli aspartate transcarbamoylase. Biochemistry 28:1617-1626.
32. Monaco HL, Crawford JL, Lipscomb WN. 1978. Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate. Proc Natl Acad Sci USA 75:5276-5280.
33. Newton CJ, Kantrowitz ER. 1990. The importance of domain closure for the allosteric transition in Escherichia coli aspartate transcarbamoylase. Biochemistry 29:1444-1451.
34. Nowlan SF, Kantrowitz ER. 1985. Superproduction and rapid purification of E. coli aspartate transcarbamoylase and its catalytic subunit under extreme derepression of the pyrimidine pathway. J Biol Chem 260:14712-14716.
35. Pastra-Landis SC, Foote J, Kantrowitz ER. 1981. An improved colorimetric assay for aspartate and ornithine transcarbamylases. Anal Biochem 118:358-363.
36. Porter RW, Modebe MO, Stark GR. 1969. Aspartate transcarbamylase: Kinetic studies of the catalytic subunit. J Biol Chem 244:1846-1859.
37. Robey EA, Schachman HK. 1985. Regeneration of active enzyme by formation of hybrids from inactive derivatives: Implications for active sites shared between polypeptide chains of aspartate transcarbamoylase. Proc Natl Acad Sci USA 82:361-365.
38. Robey EA, Wente SR, Markby DW, Flint A, Yang YR, Schachman HK. 1986. Effect of amino acid substitutions on the catalytic and regulatory properties of aspartate transcarbamoylase. Proc Natl Acad Sci USA 83:5935-5938.
39. Sanger F, Nicklen S, Coulson AR. 1977. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74:5463-5467.
40. Schachman HK. 1988. Can a simple model account for the allosteric transition of aspartate transcarbamylase. J Biol Chem 265:18583-18586.
41. Smith KA, Nowlan SF, Middleton SA, O'Donovan C, Kantrowitz ER. 1986. Involvement of tryptophan 209 in the allosteric interactions of Escherichia coli aspartate transcarbamylase using single amino acid substitution mutants. J Mol Biol 189:227-238.
42. Stebbins JW, Robertson DE, Roberts MF, Stevens RC, Lipscomb WN, Kantrowitz ER. 1992. Arginine 54 in the active site of Escherichia coli aspartate transcarbamoylase is critical for catalysis: A site-specific mutagenesis, NMR and X-ray crystallographic study. Protein Sci 1:1435-1446.
43. Stebbins JW, Xu W, Kantrowitz ER. 1989. Three residues involved in binding and catalysis in the carbamyl phosphate binding site of Escherichia coli aspartate transcarbamylase. Biochemistry 28:2592-2600.
44. Stebbins JW, Zhang Y, Kantrowitz ER. 1990. The importance of residues Arg-167 and Gln-231 in both the allosteric and catalytic mechanisms of Escherichia coli aspartate transcarbamylase. Biochemistry 29:3821-3827.
45. Stevens RC, Chook YM, Cho CY, Lipscomb WN, Kantrowitz ER. 1991. Escherichia coli aspartate carbamoyltransferase: The probing of crystal structure analysis via site-specific mutagenesis. Protein Eng 4:391-408.
46. Vieira J, Messing J. 1987. Production of single-stranded plasmid DNA. Methods Enzymol 153:3-11.
47. Wente SR, Schachman HK. 1987. Shared active sites in oligomeric enzymes: Model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis. Proc Natl Acad Sci USA 84:31-35.
48. Wu CW, Hammes GG. 1973. Relaxation spectra of aspartate transcarbamylase. Interaction of the native enzyme with an adenosine 5′-triphosphate analog. Biochemistry 12:1400-1408.
49. Xu W, Kantrowitz ER. 1989. Function of Threonine-55 in the carbamoyl phosphate binding site of Escherichia coli aspartate transcarbamoylase. Biochemistry 28:9937-9943.
50. Xu W, Kantrowitz ER. 1991. Function of serine-52 and serine-80 in the catalytic mechanism of Escherichia coli aspartate trancarbamoylase. Biochemistry 50:2535-2542.
51. Xu W, Pitts MA, Middleton SA, Kelleher SA, Kantrowitz ER. 1988. Propagation of allosteric changes through the catalytic-regulatory interface of Escherichia coli aspartate transcarbamylase. Biochemistry 27:5507-5515.