The biosynthesis of GDP-L-colitose: C-3 deoxygenation is catalyzed by a unique coenzyme B6-dependent enzyme

Journal of the American Chemical Society

Volumn 125, Issue 19, 2003, Pages 5584-5585

  Beyer, Noelle ^a,b   Alam, Jenefer ^a,b   Hallis, Tina M ^a,b,c   Guo, Zhihong ^a,b,d   Liu, Hung wen ^a,b  

^a UNIVERSITY OF TEXAS AT AUSTIN   (United States)

^b University of Minnesota   (United States)

^c INVITROGEN CORPORATION   (United States)

^d HONG KONG UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Hong Kong)

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE DIPHOSPHATE; GUANOSINE DIPHOSPHATE LEVO COLITOSE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BIOSYNTHESIS; CATALYSIS; COENZYME; GENE CLUSTER; GENE FUNCTION; GENE SEQUENCE; MOLECULAR CLONING; OPEN READING FRAME; OXYGENATION; REDUCTION; SEQUENCE HOMOLOGY;

GUANOSINE DIPHOSPHATE SUGARS; IRON-SULFUR PROTEINS; OXIDATION-REDUCTION; OXIDOREDUCTASES; VITAMIN B 6; YERSINIA PSEUDOTUBERCULOSIS;

EID: 0037621444     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja030088r     Document Type: Article

References (27)

1. (a) Whitfield, C. Trends Microbiol. 1995, 3, 178-185.
2. (b) Saito, T.; Hatada, M.; Iwanaga, S.; Kawabata, S. J. Biol. Chem. 1997, 272, 30703-30708.
3. (a) Weigel, T. M.; Liu, L.-d.; Liu, H.-w. Biochemistry 1992, 31, 2129-2139.
4. (b) Weigel, T. M.; Miller, V. P.; Liu, H.-w. Biochemistry 1992, 31, 2140- 2147.
5. (c) Thorson, J. S.; Liu, H.-w. J. Am. Chem. Soc. 1993, 115, 7539-7540.
6. (a) Miller, V. P.; Thorson, J. S.; Lo, S. F.; Ploux, O.; Liu, H.-w. Biochemistry 1993, 32, 11934-11942.
7. (b) Lo, S. F.; Miller, V. P.; Lei, Y.; Thorson, J. S.; Liu, H.-w.; Schottel, J. L. J. Bacteriol. 1994, 176, 460-468.
8. (a) Liu, H.-w.; Thorson, J. S. Annu. Rev. Microbiol. 1994, 48, 223-256.
9. (b) Hallis, T. M.; Liu, H.-W. Acc. Chem. Res. 1999, 32, 579-588.
10. (c) He, X.; Agnihotri, G.; Liu, H.-w. Chem. Rev. 2000, 100, 4615-4661.
11. (d) He, X.; Liu, H.-w. Annu. Rev. Biochem. 2002, 71, 701-754.
12. Elbein, A. D.; Heath, E. C. J. Biol. Chem. 1965, 240, 1926-1931.
13. The genes responsible for colitose biosynthesis in the Escherichia coli 0111 O-antigen have also been reported. The translated sequence of cold and that of its homologue in E. coli, wbdK, show excellent similarity (71% identity and 82% similarity) (Bastin, D. A.; Reeves, P. R. Gene 1995, 764, 17-23).
14. Thorson, J. S.; Lo, S. F.; Ploux, O.; He, X.; Liu, H.-w. J. Bacteriol. 1994, 176, 5483-5493.
15. r of 75.5 kDa estimated by gel filtration and a calculated mass of 44.5 kDa per monomer indicate that ColD exists as a homodimer in its native state.
16. (a) Lei, Y.; Ploux, O.; Liu, H.-w. Biochemistry 1995, 34, 4643-4654.
17. (b) Pascarella, S.; Bossa, F. Protein Sci. 1994, 3, 701-705.
18. A typical assay mixture contained 1.8 mM GDP-mannose, 40 μM PLP, 2 mM L-glutamate, 1.5 μM ColB, and 0.65 μM ColD in 200 μL of 50 mM potassium phosphate buffer (pH 7.0). The incubation was conducted at 37 °C for 30 min. The resulting mixture was separated by HPLC on an Econosil C18 column (4.6 × 250 mm) which was eluted isocratically with 2% acetonitrile in 50 mM triethylammonium acetate buffer (pH 6.8). The flow rate was 1 mL/min, and the detector was set at 254 nm. Retention times of the substrate and products were as follows: GDP-mannose (2), 5.1 min; GDP-4-keto-6-deoxy-mannose (3), 6.2 min; GDP-4-keto- 3,6-dideoxymannose (4), 8.8 min.
19. 6 Catalysis; A. R. Liss: New York, 1984.
20. 6 Pyridoxal Phosphate, Chemical, Biochemical, and Medical Aspects; Wiley-Interscience: New York, 1986; Parts A and B.
21. (c) John, R. A. Biochim. Biophys. Acta 1995. 1248, 81-96.
22. A large scale incubation contained 47.5 mM GDP-mannose, 1.5 mM PLP, 32.4 mM L-glutamate, 0.13 mM ColB, 3.46 μM ColD in 250 μL of 50 mM sodium phosphate buffer (pH 7.0). The incubation was conducted at 37 °C overnight. The proteins were removed by filtration through a microcon YM-10 membrane, and the filtrate was purified by HPLC using an Econosil C18 column (10 × 250 mm) as described above in ref 10. The pooled fractions containing product 4 were desalted using two consecutive Econo-Pac 10 DG (Bio-rad) columns, and product elution was achieved using water. The purified 4, after lyophilization, was stored at -80 °C.
23. + 570.0639, found m/z 570.0636.
24. -1, respectively.
25. 6 Pyridoxal Phosphate, Chemical, Biochemical, and Medical Aspects; Dolphin, D., Poulson, R., Avramovic, O., Eds.; Wiley-Interscience: New York, 1986; Part B, pp 253-310.
26. (b) Hayashi, H. J. Biochem. 1995, 118, 463-473.
27. Johnson, D. A.; Liu, H.-w. In The Biology-Chemistry Interface: A Tribute to Koji Nakanishi; Cooper, R., Snyder, J. D., Eds.; Marcel Dekker: New York, 1999; pp 351-396.