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Thiol-disulfide organization in alliin lyase (alliinase) from garlic (Allium sativum)

  1. Lev Weiner1,
  2. Irina Shin2,
  3. Linda J. W. Shimon1,
  4. Talia Miron2,
  5. Meir Wilchek2,
  6. David Mirelman2,
  7. Felix Frolow3,4,*,
  8. Aharon Rabinkov2,*

Article first published online: 2 DEC 2008

DOI: 10.1002/pro.10

Issue

Protein Science

Protein Science

Volume 18, Issue 1, pages 196–205, January 2009

Additional Information

How to Cite

Weiner, L., Shin, I., Shimon, L. J. W., Miron, T., Wilchek, M., Mirelman, D., Frolow, F. and Rabinkov, A. (2009), Thiol-disulfide organization in alliin lyase (alliinase) from garlic (Allium sativum). Protein Science, 18: 196–205. doi: 10.1002/pro.10

Author Information

  1. 1

    Department of Chemical Research Support, The Weizmann Institute of Science, 76100 Rehovot, Israel

  2. 2

    Department of Biological Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel

  3. 3

    Department of Molecular Microbiology and Biotechnology, Tel Aviv University, 69978 Tel Aviv, Israel

  4. 4

    The Daniella Rich Institute for Structural Biology, Tel Aviv University, 69978 Tel Aviv, Israel

*Department of Molecular Microbiology and Biotechnology, Tel Aviv University, 69978 Tel Aviv, Israel

Publication History

  1. Issue published online: 16 DEC 2008
  2. Article first published online: 2 DEC 2008
  3. Accepted manuscript online: 2 DEC 2008 12:00AM EST
  4. Manuscript Accepted: 7 OCT 2008
  5. Manuscript Revised: 16 SEP 2008
  6. Manuscript Received: 18 JUN 2008

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References

  • 1
    Van Damme EJ, Smeets K, Torrekens S, Van Leuven F, Peumans WJ ( 1992) Isolation and characterization of alliinase cDNA clones from garlic (Allium sativum L.) and related species. Eur J Biochem 209: 751–757.
    Direct Link:
  • 2
    Rabinkov A, Zhu XZ, Grafi G, Galili G, Mirelman D ( 1994) Alliin lyase (alliinase) from garlic (Allium sativum)—biochemical characterization and Cdna cloning. Appl Biochem Biotechnol 48: 149–171.
  • 3
    Kuettner EB, Hilgenfeld R, Weiss MS ( 2002) Purification, characterization, and crystallization of alliinase from garlic (vol. 402, p 192, 2002). Arch Biochem Biophys 404: 339–339.
  • 4
    Kuettner EB, Hilgenfeld R, Weiss MS ( 2002) The active principle of garlic at atomic resolution. J Biol Chem 277: 46402–46407.
  • 5
    Shimon LJ, Rabinkov A, Shin I, Miron T, Mirelman D, Wilchek M, Frolow F ( 2007) Two structures of alliinase from Alliium sativum L.: apo form and ternary complex with aminoacrylate reaction intermediate covalently bound to the PLP cofactor. J Mol Biol 366: 611–625.
  • 6
    Shimon LJW, Rabinkov A, Miron T, Mirelman D, Wilchek M, Frolow F ( 2002) Alliin lyase (alliinase) from garlic (Allium sativum): crystallization and preliminary X-ray characterization. Acta Crystallogr D Biol Crystallogr 58: 1335–1337.
    Direct Link:
  • 7
    Block E ( 1992) The organosulfur chemistry of the genus Allium—implications for the organic chemistry of sulfur. Angew Chem 31: 1135–1178.
    Direct Link:
  • 8
    Lawson HPKLD ( 1996) Garlic: the science and therapeutic application of Allium sativum L. and related species, 2nd ed. Baltimore, MD: Williams & Wilkins.
  • 9
    Rahman MS ( 2007) Allicin and other functional active components in garlic: health benefits and bioavailability. Int J Food Prop 10: 245–268.
  • 10
    Cavallito CJ, Bailey JH ( 1944) Allicin, the antibacterial principle of Allium sativum. I. Isolation, physical properties and antibacterial action. J Am Chem Soc 66: 1950–1951.
  • 11
    Wills ED ( 1956) Enzyme inhibition by allicin, the active principle of garlic. Biochem J 63: 514–520.
  • 12
    Han J, Lawson L, Han G, Han P ( 1995) A spectrophotometric method for quantitative determination of allicin and total garlic thiosulfinates. Anal Biochem 225: 157–160.
  • 13
    Rabinkov A, Miron T, Konstantinovski L, Wilchek M, Mirelman D, Weiner L ( 1998) The mode of action of allicin: trapping of radicals and interaction with thiol containing proteins. Biochim Biophys Acta 1379: 233–244.
  • 14
    Millard CB, Shnyrov VL, Newstead S, Shin I, Roth E, Silman I, Weiner L ( 2003) Stabilization of a metastable state of Torpedo californica acetylcholinesterase by chemical chaperones. Protein Sci 12: 2337–2347.
    Direct Link:
  • 15
    Prager-Khoutorsky M, Goncharov I, Rabinkov A, Mirelman D, Geiger B, Bershadsky AD ( 2007) Allicin inhibits cell polarization, migration and division via its direct effect on microtubules. Cell Motil Cytoskeleton 64: 321–337.
    Direct Link:
  • 16
    Rabinkov A, Miron T, Mirelman D, Wilchek M, Glozman S, Yavin E, Weiner L ( 2000) S-Allylmercaptoglutathione: the reaction product of allicin with glutathione possesses SH-modifying and antioxidant properties. Biochim Biophys Acta 1499: 144–153.
  • 17
    Stoll A, Seebeck E ( 1951) Chemical investigation on alliin, the specific principle of garlic. Adv Enzymol 11: 377–400.
  • 18
    Mazelis M, Crews L ( 1968) Purification of the alliin lyase of garlic, Allium sativum L. Biochem J 108: 725–730.
  • 19
    Kazarian RA, Goryachenkova EV ( 1978) Alliinase: Purification and characterization. Biokhimya (Engl transl) 43: 1502–1508.
  • 20
    Torchinsky YM ( 1981) Sulfur in proteins. New York: Pergamon.
  • 21
    Tai CH, Yoon MY, Kim SK, Rege VD, Nalabolu SR, Kredich NM, Schnackerz KD, Cook PF ( 1998) Cysteine 42 is important for maintaining an integral active site for O-acetylserine sulfhydrylase resulting in the stabilization of the alpha-aminoacrylate intermediate. Biochemistry 37: 10597–10604.
  • 22
    Dominici P, Maras B, Mei G, Borri Voltattorni C ( 1991) Affinity labeling of pig kidney 3,4-dihydroxyphenylalanine (Dopa) decarboxylase with N-(bromoacetyl)pyridoxamine 5′-phosphate. Modification of an active-site cysteine. Eur J Biochem 201: 393–397.
    Direct Link:
  • 23
    Darii EL, Sukhareva BS ( 1992) Reactivation and reconstitution of glutamate decarboxylase upon the interaction of its dimers with pyridoxal phosphate. Biokhimiia 57: 574–581.
  • 24
    Conway ME, Yennawar N, Wallin R, Poole LB, Hutson SM ( 2003) Human mitochondrial branched chain aminotransferase: structural basis for substrate specificity and role of redox active cysteines. Biochim Biophys Acta 1647: 61–65.
  • 25
    Weiner LM ( 1995) Quantitative determination of thiol groups in low and high molecular weight compounds by electron paramagnetic resonance. Methods Enzymol 251: 87–105.
  • 26
    Weiner LM ( 2007) Stable nitroxyl radicals as pH, thiol and electron transfer probes. Appl Magn Reson 31: 357–373.
  • 27
    Kokorin AI, Zamaraev KI, Grigorian GL, Ivanov VP, Rozantsev EG ( 1972) Measurement of the distance between paramagnetic centers in solid solutions of nitrosyl radicals, biradicals and spin-labelled proteins. Biofizika 17: 34–41.
  • 28
    Voss J, Salwinski L, Kaback HR, Hubbell WL ( 1995) A method for distance determination in proteins using a designed metal ion binding site and site-directed spin labeling: evaluation with T4 lysozyme. Proc Natl Acad Sci USA 92: 12295–12299.
  • 29
    Mevorat-Kaplan K, Weiner L, Sheves M ( 2006) Spin labeling of Natronomonas pharaonis halorhodopsin: probing the cysteine residues environment. J Phys Chem B 110: 8825–8831.
  • 30
    Dolginova EA, Roth E, Silman I, Weiner LM ( 1992) Chemical modification of Torpedo acetylcholinesterase by disulfides: appearance of a “molten globule” state. Biochemistry 31: 12248–12254.
  • 31
    Miron T, Bercovici T, Rabinkov A, Wilchek M, Mirelman D ( 2004) [3H]Allicin: preparation and applications. Anal Biochem 331: 364–369.
  • 32
    Miron T, Rabinkov A, Mirelman D, Wilchek M, Weiner L ( 2000) The mode of action of allicin: its ready permeability through phospholipid membranes may contribute to its biological activity. Biochim Biophys Acta 1463: 20–30.
  • 33
    Manabe T, Hasumi A, Sugiyama M, Yamazaki M, Saito K ( 1998) Alliinase [S-alk(en)yl-L-cysteine sulfoxide lyase] from Allium tuberosum (Chinese chive). Eur J Biochem 257: 21–30.
    Direct Link:
  • 34
    Lancaster JE, Shaw ML, Joyce MDP, McCallum JA, McManus MT ( 2000) A novel alliinase from onion roots. Biochemical characterization and cDNA cloning. Plant Physiol 122: 1269–1279.
  • 35
    Miron T, Mironchik M, Mirelman D, Wilchek M, Rabinkov A ( 2003) Inhibition of tumor growth by a novel approach: in situ allicin generation using targeted alliinase delivery. Mol Cancer Ther 2: 1295–1301.
  • 36
    Arditti FD, Rabinkov A, Miron T, Reisner Y, Berrebi A, Wilchek M, Mirelman D ( 2005) Apoptotic killing of B-chronic lymphocytic leukemia tumor cells by allicin generated in situ using a rituximab-alliinase conjugate. Mol Cancer Ther 4: 325–331.
  • 37
    Khramtsov VV, Yelinova VI, Weiner LM, Berezina TA, Martin VV, Volodarsky LB ( 1989) Quantitative determination of SH groups in low- and high-molecular-weight compounds by an electron spin resonance method. Anal Biochem 182: 58–63.
  • 38
    Degani Y, Patchornik A ( 1971) Selective cyanylation of sulfhydryl groups. II. On the synthesis of 2-nitro-5-thiocyanatobenzoic acid. J Org Chem 36: 2727–2728.
  • 39
    Rabinkov A, Wilchek M, Mirelman D ( 1995) Garlic alliinase is glycosylated at Asn146 and forms a complex with the mannose-specific lectin from the same plant. FASEB J 9: A1361–A1361.
  • 40
    Miron T, Rabinkov A, Mirelman D, Weiner L, Wilchek M ( 1998) A spectrophotometric assay for allicin and alliinase (alliin lyase) activity: reaction of 2-nitro-5-thiobenzoate with thiosulfinates. Anal Biochem 265: 317–325.
  • 41
    Peretz M, Weiner LM, Burstein Y ( 1997) Cysteine reactivity in Thermoanaerobacter brockii alcohol dehydrogenase. Protein Sci 6: 1074–1083.
    Direct Link:
  • 42
    Shin I, Silman I, Weiner L ( 1996) Interaction of partially unfolded forms of Torpedo acetylcholinesterase with liposomes. Protein Sci 5: 42–51.
    Direct Link:
  • 43
    Emsley P, Cowtan K ( 2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126–2132.
    Direct Link:
  • 44
    DeLano WL ( 2002) The PyMOL molecular graphic system. San Carlos, CA: DeLano Scientific LLC. Available at:http://www.pymol.org.
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