Aldehyde and phosphinate analogs of glutathione and glutathionylspermidine: Potent, selective binding inhibitors of the E. coli bifunctional glutathionylspermidine synthetase/amidase

Chemistry and Biology

Volumn 4, Issue 11, 1997, Pages 859-866

  Lin, Chun Hung ^a,c   Chen, Shoujun ^b   Kwon, David S ^a   Coward, James K ^b   Walsh, Christopher T ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

^c INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

Author keywords

Glutathionylspermidine; Gsp phosphinates; Gsp synthetase amidase; Slow binding inhibitor; Glu Ala Gly aldehyde

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; TRYPANOSOMATIDAE;

EID: 0031280053     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(97)90118-6     Document Type: Article

References (18)

1. 1-glutathionylspermidine in Crithidia fasciculata. Mol. Biochem. Parasitol. 21, 247-257.
2. Smith, K., Nadeau, K., Bradley, M., Walsh, C.T. & Fairlamb, A.H. (1992). Purification of glutathionylspermidine and trypanothione synthetase from Crithidia fasciculata. Protein Sci. 1, 874-883.
3. Bollinger, J.M., Jr., Kwon, D.S., Huisman, G.W., Kolter, R. & Walsh, C.T. (1995). Glutathionylspermidine metabolism in Escherichia coli. J. Biol. Chem. 270, 14031-14041.
4. Koenig, K., Menge, U., Kiess, M., Wray, V. & Flohe, L. (1997). Convenient isolation and kinetic mechanism of glutathionylspermidine synthetase from Crithidia faciculata. J. Biol. Chem. 272, 11908-11915.
5. Fairlamb, A.H., Blackburn, P., Ulrich, P., Chait, B.T. & Cerami, A. (1985). Trypanothione: a novel bis(glutathionyl) spermidine cofactor for glutathione reductase in trypanosomatids. Science 227, 1485-1487.
6. Kwon, D.S., Lin, C.H., Chen, S., Coward, J.K., Walsh, C.T. & Bollinger, J.M., Jr (1997). Dissection of glutathionylspermidine synthetase/amidase from Escherichia coli into autonomously folding and functional synthetase and amidase domains. J. Biol. Chem. 272, 2429-2436.
7. Chen, S., Lin, C.-H., Walsh, C.T. & Coward, J.K. (1997). Novel inhibitor of trypanothione biosynthesis: synthesis and evaluation of a phosphinate analog of glutathionyl spermidine (Gsp), a potent, slow-binding inhibitor of Gsp synthetase. Bioorg. Med. Chem. Lett. 7, 505-510.
8. Lin, C.H., Kwon, D.S., Bollinger, J.M., Jr. & Walsh, C.T. (1997). Evidence for a glutathionyl-enzyme intermediate in the amidase activity of the bifunctional glutathionylspermidine synthetase/amidase from Escherichia coli. Biochemistry, in press.
9. Dufour, E., Storer, A.C. & Menard, R. (1995). Peptide aldehydes and nitriles as transition state analog inhibitors of cysteine proteases. Biochemistry. 34, 9136-9143.
10. Radzicka, A. & Wolfenden, R. (1995). Transition state and multisubstrate analog inhibitors. Methods Enzymol. 249, 284-314.
11. Kamber, B. & Rittel, W. (1968). Eine neue, einfache methods zur translation von cystinpeptiden. [A new, simple method for synthesis of cysteine peptides]. Helv. Chim. Acta. 51, 2061-2064.
12. Chen, S. & Coward, J.K. (1996). A general method for the synthesis of N-protected α-aminoalkylphosphinic acids. Tetrahedron Lett. 37, 4335-4338.
13. Rano, T.A., et al., & Thornberry, N.A. (1997). A combinatorial approach for determining protease specificities: application to interleukin-1β converting enzyme (ICE). Chem. Biol. 4, 149-155.
14. Han, Z., Hendrickson, E.A., Bremner, T.A. & Wyche, J.H. (1997). A sequential two-step mechanism for the production of the mature p17:p12 form of caspase-3 in vitro. J. Biol. Chem. 272, 13432-13436.
15. Margolin, N., et al., & Livingston, D.J. (1997). Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases. J. Biol. Chem. 272, 7223-7228.
16. Seemuller, E., Lupas, A., Stock, D., Lowe, J., Huber, R. & Baumeister, W. (1995). Proteasome from Thermoplasma acidophilum: a threonine protease. Science 268, 579-582.
17. Seemuller, E., Lupas, A. & Baumeister, W. (1996). Autocatalytic processing of the 20S proteasome. Nature 382, 468-470.
18. Akopian, T.N., Kisselev, A.F. & Goldberg, A.L. (1997). Processive degradation of proteins and other catalytic properties of the proteasome from Thermoplasma acidophilum. J. Biol. Chem. 272, 1791-1798.