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Volumn 90, Issue 1, 2012, Pages 81-88

A novel molecular mechanism to explain biotin-unresponsive holocarboxylase synthetase deficiency

Author keywords

Biotin protein ligase; Enzyme; Holocarboxylase synthetase; Multiple carboxylase deficiency; Protein interaction

Indexed keywords

BIOTIN;

EID: 84857366331     PISSN: 09462716     EISSN: 14321440     Source Type: Journal    
DOI: 10.1007/s00109-011-0811-x     Document Type: Article
Times cited : (27)

References (35)
  • 2
    • 0036183336 scopus 로고    scopus 로고
    • Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes
    • Attwood PV, Wallace JC (2002) Chemical and catalytic mechanisms of carboxyl transfer reactions in biotin-dependent enzymes. Acc Chem Res 35:113-120
    • (2002) Acc Chem Res , vol.35 , pp. 113-120
    • Attwood, P.V.1    Wallace, J.C.2
  • 3
    • 0038811689 scopus 로고    scopus 로고
    • The biotin enzyme family: Conserved structural motifs and domain rearrangements
    • DOI 10.2174/1389203033487199
    • Jitrapakdee S, Wallace JC (2003) The biotin enzyme family: conserved structural motifs and domain rearrangements. Curr Protein Pept Sci 4:217-229 (Pubitemid 36656735)
    • (2003) Current Protein and Peptide Science , vol.4 , Issue.3 , pp. 217-229
    • Jitrapakdee, S.1    Wallace, J.C.2
  • 4
    • 0018639436 scopus 로고
    • Biotin-response organicaciduria. Multiple carboxylase defects and complementation studies with propionicacidemia in cultured fibroblasts
    • Saunders M, Sweetman L, Robinson B, Roth K, Cohn R, Gravel RA (1979) Biotin-response organicaciduria. Multiple carboxylase defects and complementation studies with propionicacidemia in cultured fibroblasts. J Clin Invest 64:1695-1702 (Pubitemid 10181312)
    • (1979) Journal of Clinical Investigation , vol.64 , Issue.6 , pp. 1695-1702
    • Saunders, M.1    Sweetman, L.2    Robinson, B.3
  • 6
    • 0003114965 scopus 로고
    • Disorders of biotin metabolism
    • Beavder AL, Sly WS, Scriver CR (eds) . McGraw-Hill, New York
    • Wolf B (1995) Disorders of biotin metabolism. In: Beavder AL, Sly WS, Scriver CR (eds) The metabolic and molecular basis of inherited diseases. McGraw-Hill, New York, pp 3151-3177
    • (1995) The Metabolic and Molecular Basis of Inherited Diseases , pp. 3151-3177
    • Wolf, B.1
  • 8
    • 22144447164 scopus 로고    scopus 로고
    • Severe holocarboxylase synthetase deficiency with incomplete biotin responsiveness resulting in antenatal insult in Samoan neonates
    • DOI 10.1016/j.jpeds.2005.03.006, PII S0022347605001988
    • Wilson CJ, Myer M, Darlow BA, Stanley T, Thomson G, Baumgartner ER, Kirby DM, Thorburn DR (2005) Severe holocarboxylase synthetase deficiency with incomplete biotin responsiveness resulting in antenatal insult in samoan neonates. J Pediatr 147:115-118 (Pubitemid 40981157)
    • (2005) Journal of Pediatrics , vol.147 , Issue.1 , pp. 115-118
    • Wilson, C.J.1    Myer, M.2    Darlow, B.A.3    Stanley, T.4    Thomson, G.5    Baumgartner, E.R.6    Kirby, D.M.7    Thorburn, D.R.8
  • 10
    • 25444442591 scopus 로고    scopus 로고
    • Mutations in the holocarboxylase synthetase gene HLCS
    • DOI 10.1002/humu.20204
    • Suzuki Y, Yang X, Aoki Y, Kure S, Matsubara Y (2005) Mutations in the holocarboxylase synthetase gene HLCS. Hum Mutat 26:285-290 (Pubitemid 41361794)
    • (2005) Human Mutation , vol.26 , Issue.4 , pp. 285-290
    • Suzuki, Y.1    Yang, X.2    Aoki, Y.3    Kure, S.4    Matsubara, Y.5
  • 11
    • 0032966097 scopus 로고    scopus 로고
    • Bioavailability of biotin given orally to humans in pharmacologic doses
    • Zempleni J,Mock DM(1999) Bioavailability of biotin given orally to humans in pharmacologic doses. Am J Clin Nutr 69:504-508 (Pubitemid 29104573)
    • (1999) American Journal of Clinical Nutrition , vol.69 , Issue.3 , pp. 504-508
    • Zempleni, J.1    Mock, D.M.2
  • 12
    • 0019440979 scopus 로고
    • Multiple carboxylase deficiency: Clinical and biochemical improvement following neonatal biotin treatment
    • Wolf B, Hsia YE, Sweetman L, Feldman G, Boychuk RB, Bart RD, Crowell DH, Di Mauro RM, Nyhan WL (1981) Multiple carboxylase deficiency: clinical and biochemical improvement following neonatal biotin treatment. Pediatrics 68:113-118 (Pubitemid 11061376)
    • (1981) Pediatrics , vol.68 , Issue.1 , pp. 113-118
    • Wolf, B.1    Hsia, Y.E.2    Sweetman, L.3
  • 14
    • 0032809640 scopus 로고    scopus 로고
    • Mechanism of biotin responsiveness in biotin-responsive multiple carboxylase deficiency
    • DOI 10.1006/mgme.1998.2785
    • Dupuis L, Campeau E, Leclerc D, Gravel RA (1999) Mechanism of biotin responsiveness in biotin-responsive multiple carboxylase deficiency. Mol Gen Metabol 66:80-90 (Pubitemid 29390212)
    • (1999) Molecular Genetics and Metabolism , vol.66 , Issue.2 , pp. 80-90
    • Dupuis, L.1    Campeau, E.2    Leclerc, D.3    Gravel, R.A.4
  • 16
    • 0022439250 scopus 로고
    • Inheritable biotin-treatable disorders and associated phenomena
    • Sweetman L, Nyhan WL (1986) Inheritable biotin-treatable disorders and associated phenomena. Annu Rev Nutr 6:317-343
    • (1986) Annu Rev Nutr , vol.6 , pp. 317-343
    • Sweetman, L.1    Nyhan, W.L.2
  • 20
    • 25144501423 scopus 로고    scopus 로고
    • Crystal structures of biotin protein ligase from Pyrococcus horikoshii OT3 and its complexes: Structural basis of biotin activation
    • DOI 10.1016/j.jmb.2005.08.032, PII S0022283605009691
    • Bagautdinov B, Kuroishi C, Sugahara M, Kunishima N (2005) Crystal structures of biotin protein ligase from Pyrococcus horikoshii OT3 and its complexes: structural basis of biotin activation. J Mol Biol 353:322-333 (Pubitemid 41356615)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.2 , pp. 322-333
    • Bagautdinov, B.1    Kuroishi, C.2    Sugahara, M.3    Kunishima, N.4
  • 21
    • 0026666377 scopus 로고
    • Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains
    • Wilson KP, Shewchuk LM, Brennan RG, Otsuka AJ, Matthews BW (1992) Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc Natl Acad Sci USA 89:9257-9261
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 9257-9261
    • Wilson, K.P.1    Shewchuk, L.M.2    Brennan, R.G.3    Otsuka, A.J.4    Matthews, B.W.5
  • 22
    • 0035853728 scopus 로고    scopus 로고
    • Expression in Escherichia coli of N- and C-terminally deleted human holocarboxylase synthetase. Influence of the N-terminus on biotinylation and identification of a minimum functional protein
    • Campeau E, Gravel RA (2001) Expression in Escherichia coli of N- and C-terminally deleted human holocarboxylase synthetase. Influence of the N-terminus on biotinylation and identification of a minimum functional protein. J Biol Chem 276:12310-12316
    • (2001) J Biol Chem , vol.276 , pp. 12310-12316
    • Campeau, E.1    Gravel, R.A.2
  • 23
    • 61849137804 scopus 로고    scopus 로고
    • N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition
    • Hassan YI, Moriyama H, Olsen LJ, Bi X, Zempleni J (2009) N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition. Mol Genet Metabol 96:183-188
    • (2009) Mol Genet Metabol , vol.96 , pp. 183-188
    • Hassan, Y.I.1    Moriyama, H.2    Olsen, L.J.3    Bi, X.4    Zempleni, J.5
  • 24
    • 71449118660 scopus 로고    scopus 로고
    • Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition
    • Ingaramo M, Beckett D (2009) Distinct amino termini of two human HCS isoforms influence biotin acceptor substrate recognition. J Biol Chem 284:30862-30870
    • (2009) J Biol Chem , vol.284 , pp. 30862-30870
    • Ingaramo, M.1    Beckett, D.2
  • 25
    • 77649270119 scopus 로고    scopus 로고
    • The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein
    • Lee CK, Cheong C, Jeon YH (2010) The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein. FEBS Lett 584:675-680
    • (2010) FEBS Lett , vol.584 , pp. 675-680
    • Lee, C.K.1    Cheong, C.2    Jeon, Y.H.3
  • 26
    • 45049083010 scopus 로고    scopus 로고
    • Reduced half-life of holocarboxylase synthetase from patients with severe multiple carboxylase deficiency
    • Bailey LM, Ivanov RA, Jitrapakdee S, Wilson CJ, Wallace JC, Polyak SW (2008) Reduced half-life of holocarboxylase synthetase from patients with severe multiple carboxylase deficiency. Hum Mutat 29:E47-57
    • (2008) Hum Mutat , vol.29
    • Bailey, L.M.1    Ivanov, R.A.2    Jitrapakdee, S.3    Wilson, C.J.4    Wallace, J.C.5    Polyak, S.W.6
  • 27
    • 0030702915 scopus 로고    scopus 로고
    • Characterization of mutant holocarboxylase synthetase (HCS)-a Km for biotin was not elevated in a patient with HCS deficiency
    • Aoki Y, Suzuki Y, Li X, Sakamoto O, Chikaoka H, Takita S, Narisawa K (1997) Characterization of mutant holocarboxylase synthetase (HCS)-a Km for biotin was not elevated in a patient with HCS deficiency. Ped Res 42:849-854
    • (1997) Ped Res , vol.42 , pp. 849-854
    • Aoki, Y.1    Suzuki, Y.2    Li, X.3    Sakamoto, O.4    Chikaoka, H.5    Takita, S.6    Narisawa, K.7
  • 28
    • 0033590217 scopus 로고    scopus 로고
    • Functional expression, purification, and characterization of recombinant human pyruvate carboxylase
    • DOI 10.1006/bbrc.1999.1846
    • Jitrapakdee S, Walker ME, Wallace JC (1999) Functional expression, purification, and characterization of recombinant human pyruvate carboxylase. Biochem Biophys Res Commun 266:512-517 (Pubitemid 30028698)
    • (1999) Biochemical and Biophysical Research Communications , vol.266 , Issue.2 , pp. 512-517
    • Jitrapakdee, S.1    Walker, M.E.2    Wallace, J.C.3
  • 29
    • 0032731352 scopus 로고    scopus 로고
    • Biotin protein ligase from Saccharomyces cerevisiae: The N-terminal domain is required for complete activity
    • Polyak SW, Chapman-Smith A, Brautigan PJ, Wallace JC (1999) Biotin protein ligase from Saccharomyces cerevisiae. The N-terminal domain is required for complete activity. J Biol Chem 274:32847-32854 (Pubitemid 129535319)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.46 , pp. 32847-32854
    • Polyak, S.W.1    Chapman-Smith, A.2    Brautigan, P.J.3    Wallace, J.C.4
  • 30
    • 0035793573 scopus 로고    scopus 로고
    • Mutational analysis of protein substrate presentation in the post-translational attachment of biotin to biotin domains
    • Polyak SW, Chapman-Smith A, Mulhern TD, Cronan JE Jr, Wallace JC (2001) Mutational analysis of protein substrate presentation in the post-translational attachment of biotin to biotin domains. J Biol Chem 276:3037-3045
    • (2001) J Biol Chem , vol.276 , pp. 3037-3045
    • Polyak, S.W.1    Chapman-Smith, A.2    Mulhern, T.D.3    Cronan Jr., J.E.4    Wallace, J.C.5
  • 31
    • 21644455793 scopus 로고    scopus 로고
    • 15 N resonance assignments of the third spectrin repeat of α-actinin-4 [2]
    • DOI 10.1023/B:JNMR.0000034342.20537.01
    • 15N resonance assignments of the third spectrin repeat of alphaactinin-4. J Biomol NMR 29:533-534 (Pubitemid 38967365)
    • (2004) Journal of Biomolecular NMR , vol.29 , Issue.4 , pp. 533-534
    • Kowalski, K.1    Merkel, A.L.2    Booker, G.W.3
  • 32
    • 0029565346 scopus 로고
    • Evidence for distinct ligand-bound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis
    • DOI 10.1021/bi00051a010
    • Xu Y, Nenortas E, Beckett D (1995) Evidence for distinct ligandbound conformational states of the multifunctional Escherichia coli repressor of biotin biosynthesis. Biochemistry 34:16624-16631 (Pubitemid 26011785)
    • (1995) Biochemistry , vol.34 , Issue.51 , pp. 16624-16631
    • Xu, Y.1    Nenortas, E.2    Beckett, D.3
  • 33
    • 34548605606 scopus 로고    scopus 로고
    • Nucleation of an Allosteric Response via Ligand-induced Loop Folding
    • DOI 10.1016/j.jmb.2007.07.020, PII S0022283607009576
    • Naganathan S, Beckett D (2007) Nucleation of an allosteric response via ligand-induced loop folding. J Mol Biol 373:96-111 (Pubitemid 47398877)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.1 , pp. 96-111
    • Naganathan, S.1    Beckett, D.2
  • 34
    • 0037474538 scopus 로고    scopus 로고
    • Coupling of protein assembly and DNA binding: Biotin repressor dimerization precedes biotin operator binding
    • DOI 10.1016/S0022-2836(02)01308-6
    • Streaker ED, Beckett D (2003) Coupling of protein assembly and DNA binding: biotin repressor dimerization precedes biotin operator binding. J Mol Biol 325:937-948 (Pubitemid 36263405)
    • (2003) Journal of Molecular Biology , vol.325 , Issue.5 , pp. 937-948
    • Streaker, E.D.1    Beckett, D.2
  • 35
    • 77950461420 scopus 로고    scopus 로고
    • Holocarboxylase synthetase: Correlation of protein localisation with biological function
    • Bailey LM, Wallace JC, Polyak SW (2010) Holocarboxylase synthetase: correlation of protein localisation with biological function. Arch Biochem Biophys 496:45-52
    • (2010) Arch Biochem Biophys , vol.496 , pp. 45-52
    • Bailey, L.M.1    Wallace, J.C.2    Polyak, S.W.3


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