Expression, purification, and characterization of stable, recombinant human adenylosuccinate lyase

Protein Expression and Purification

Volumn 51, Issue 2, 2007, Pages 227-234

  Lee, Peychii ^a   Colman, Roberta F ^a  

^a UNIVERSITY OF DELAWARE   (United States)

Author keywords

Adenylosuccinate lyase; ADL deficiency; His tagged enzyme; Human adenylosuccinate lyase

Indexed keywords

ADENOSINE PHOSPHATE; ADENYLOSUCCINATE LYASE; ADENYLOSUCCINIC ACID; DRUG DERIVATIVE; RECOMBINANT PROTEIN; THIOL DERIVATIVE;

ARTICLE; BIOSYNTHESIS; CIRCULAR DICHROISM; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; HUMAN; ISOLATION AND PURIFICATION; KINETICS; METABOLISM; MOLECULAR CLONING; OXIDATION REDUCTION REACTION; PH; PROTEIN QUATERNARY STRUCTURE; PROTEIN SECONDARY STRUCTURE; TEMPERATURE;

ADENOSINE MONOPHOSPHATE; ADENYLOSUCCINATE LYASE; CIRCULAR DICHROISM; CLONING, MOLECULAR; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; OXIDATION-REDUCTION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SULFHYDRYL COMPOUNDS; TEMPERATURE;

ESCHERICHIA COLI;

EID: 33751434986     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.07.023     Document Type: Article

References (33)

1. Ebbole D.J., and Zalkin H. Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis. J. Biol. Chem. 262 (1987) 8274-8287
2. Toth E.A., Worby C., Dixon J.E., Goedken E.R., Marqusee S., and Yeates T.O. The crystal structure of adenylosuccinate lyase from Pyrobaculum aerophilum reveals an intracellular protein with three disulfide bonds. J. Mol. Biol. 301 (2000) 433-450
3. Toth E.A., and Yeates T.O. The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway. Structure 8 (2000) 163-174
4. Aimi J., Badylak J., Williams J., Chen Z., Zalkin H., and Dixon J.E. Cloning of a cDNA encoding adenylosuccinate lyase by functional complementation in Escherichia coli. J. Biol. Chem. 265 (1990) 9011-9014
5. Wang L.-J.C., and O'Brien W.E. Characterization of the cDNA and the gene encoding murine adenylosuccinate lyase. Genomics 28 (1995) 341-343
6. Redinbo M.R., Eide S.M., Stone R.L., Dixon J.E., and Yeates T.O. Crystallization and preliminary structural analysis of Bacillus subtilis adenylosuccinate lyase, an enzyme implicated in infantile autisum. Protein Sci. 5 (1996) 786-788
7. Stone R.L., Aimi J., Barshop B.A., Jacken J., Van den Berghe G., Zalkin H., and Dixon J.E. A mutation in adenylosuccinate lyase associated with mental retardation and autistic features. Nat. Genet. 1 (1992) 59-63
8. Van Keuren M.L., Hart I.M., Kao F.T., Neve R.L., Bruns G.A., Kurnit D.M., and Patterson D. A somatic cell hybrid with a single human chromosome 22 corrects the defect in the CHO mutant (Ade-1) lacking adenylosuccinase activity. Cytogenet. Cell Genet. 44 (1987) 142-147
9. Delattre O., Azambuja C.J., Aurias A., Zucman J., Peter M., Zhang F., Hors-Cayla M.C., Rouleau G., and Thomas G. Mapping of human chromosome 22 with a panel of somatic cell hybrids. Genomics 9 (1991) 721-727
10. Fon E.A., Demczuk S., Delattre O., Thomas G., and Rouleau G.A. Mapping of human adenylosuccinate lyase (ADSL) gene to chromosome 22q13.1 → q13.2. Cytogenet. Cell Genet. 64 (1993) 201-203
11. Van den Berghe G., and Jaeken J. Adenylosuccinate lyase deficiency. In: Scriver C.P., Beaudet A.L., Sly W.S., Valle D., Childs B., Kinzler K.W., and Vogelstein B. (Eds). The Metabolic and Molecular Basis of Inherited Diseases. 8th ed. vol. II (2001), McGraw-Hill, N.Y. 2653-2662
12. Spiegel E.K., Colman R.F., and Patterson D. Adenylosuccinate lyase deficiency. Mol. Genet. Met. 89 (2006) 19-31
13. Kmoch S., Hartmannova H., Stiburkova B., Krijt J., Zikanova M., and Sebesta I. Human adenylosuccinate lyase (ADSL), cloning and characterization of full-length cDNA and its isoform, gene structure and molecular basis for ADSL deficiency in six patients. Hum. Mol. Genet. 9 (2000) 1501-1513
14. Race V., Marie S., Vincent M.-F., and Van den Berghe G. Clinical, biochemical and molecular genetic correlations in adenylosuccinate lyase deficiency. Hum. Mol. Genet. 9 (2000) 2159-2165
15. Butkowski R.J., Elion J., Downing M.R., and Mann K.G. Primary structure of human prethrombin 2 and α-thrombin. J. Biol. Chem. 252 (1977) 4942-4957
16. 141 in the active site of Bacillus subtilis adenylosuccinate lyase by affinity labeling with 6-(4-bromo-2,3-dioxobutyl)thioadenosine 5′-monophosphate. J. Biol. Chem. 272 (1997) 458-465
17. Palenchar J.B., and Colman R.F. Characterization of a mutant Bacillus subtilis adenylosuccinate lyase equivalent to a mutant enzyme found in human adenylosuccinate lyase deficiency: asparagine 276 plays an important structural role. Biochemistry 42 (2003) 1831-1841
18. Poole L.B. Flavin-dependent alkyl hydroperoxide reductase from Salmonella typhimurium. 2. Cystine disulfides involved in catalysis of peroxide reduction. Biochemistry 35 (1996) 65-75
19. Riddles P.W., Blakeley R.L., and Zerner B. Ellman's reagent: 5,5′-dithiobis(2-nitrobenzoic acid); A reexamination. Anal. Biochemistry 94 (1979) 75-81
20. Schneider J.P., Lear J.D., and DeGrado W.F. A designed buried salt bridge in a heterodimeric coiled coil. J. Am. Chem. Soc. 119 (1997) 5742-5743
21. Kretsinger J.K., and Schenider J.P. Design and application of basic amino acid displaying enhanced hydrophobicity. J. Am. Chem. Soc. 125 (2003) 7907-7913
22. Rudolph R., and Lilie H. In vitro folding of inclusion body proteins. FASEB J. 10 (1996) 49-56
23. Rogl H., Kosemund K., Kuhlbrandt W., and Collinson I. Refolding of Escherichia coli produced membrane protein inclusion bodies immobilised by nickel chelating chromatography. FEBS Lett. 432 (1998) 21-26
24. Zahn R., von Schroetter C., and Wuthrich K. Human prion proteins expressed in Escherichia coli and purified by high-affinity column refolding. FEBS Lett. 417 (1997) 400-404
25. Lilie H., Schwarz E., and Rudolph R. Advances in refolding of proteins produced in E. coli. Curr. Opin. Biotech. 9 (1998) 497-501
26. Stone R.L., Zalkin H., and Dixon J.E. Expression, purification, and kinetic characterization of recombinant human adenylosuccinate lyase. J. Biol. Chem. 268 (1993) 19710-19716
27. Gite S.U., and Colman R.F. Affinity labeling of the active site of rabbit muscle adenylosuccinate lyase by 2-[(4-bromo-2,3-dioxobutyl)thio]adenosine 5′-monophosphate. Biochemistry 35 (1996) 2658-2667
28. Edery P., Chabrier S., Ceballos-Picot I., Marie S., Vincent M.-F., and Tardieu M. Intrafamilial variability in the phenotypic expression of adenylosuccinate lyase deficiency: a report on three patients. Am. J. Med. Genet. A120 (2003) 185-190
29. Marinaki A.M., Champion M., Kurian M.A., Simmonds H.A., Marie S., Vincent M.F., Van den Berghe G., Duley J.A., and Fairbanks L.D. Adenylosuccinate lyase deficiency-first British case. Nucleosides Nucleotides Nucleic Acids 23 (2004) 1231-1233
30. Lee T.T., Worby C., Bao Z.-Q., Dixon J.E., and Colman R.F. His68 and His141 are critical contributors to the intersubunit catalytic site of adenylosuccinate lyase of Bacillus subtilis. Biochemistry 38 (1999) 22-32
31. Brosius J.L., and Colman R.F. A key role in catalysis for His89 of adenylosuccinate lyase of Bacillus subtilis. Biochemistry 39 (2000) 13336-13343
32. Palenchar J.B., Crocco J.M., and Colman R.F. The characterization of mutant Bacillus subilis adenylosuccinate lyases corresponding to severe human adenylosuccinate lyase deficiencies. Protein Sci. 12 (2003) 1694-1705
33. Sivendran S., Patterson D., Spiegel E., McGown I., Cowley D., and Colman R.F. Two novel mutant human adenylosuccinate lyase (ASLs) associated with autism and characterization of the equivalent mutant Bacillus subtilis ASL. J. Biol. Chem. 279 (2004) 53789-53797