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Volumn 185, Issue 4, 2006, Pages 297-306

Erratum: 3-Methylglutaconyl-CoA hydratase from Acinetobacter sp (Archives of Microbiology (2006) DOI: 10.1007/s00203-006-0095-7);3-Methylglutaconyl-CoA hydratase from Acinetobacter sp

Author keywords

(S) Leucine degradation; 3 Methylglutaconyl CoA hydratase; Acinetobacter sp.; Hydration dehydration reactions

Indexed keywords

3 METHYLGLUTACONYL COENZYME A HYDRATASE; BACTERIAL ENZYME; CARBON; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; ISOVALERIC ACID; LEUCINE; UNCLASSIFIED DRUG;

EID: 33645964931     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-006-0114-8     Document Type: Erratum
Times cited : (7)

References (34)
  • 1
    • 0037176907 scopus 로고    scopus 로고
    • Structural mechanism of enoy-CoA hydratase: Three atoms from a single water are added in either an E1cb stepwise or concerted fashion
    • Bahnson BJ, Anderson VE, Petsko GA (2002) Structural mechanism of enoy-CoA hydratase: three atoms from a single water are added in either an E1cb stepwise or concerted fashion. Biochemistry 41:2621-2629
    • (2002) Biochemistry , vol.41 , pp. 2621-2629
    • Bahnson, B.J.1    Anderson, V.E.2    Petsko, G.A.3
  • 2
    • 0033522167 scopus 로고    scopus 로고
    • Characterisation and mitochondrial localisation of AUH, an AU-specific RNA-binding enoyl-CoA hydratase
    • Brennan LE, Nakagawa J, Egger D, Bienz K, Moroni C (1999) Characterisation and mitochondrial localisation of AUH, an AU-specific RNA-binding enoyl-CoA hydratase. Gene 228:85-91
    • (1999) Gene , vol.228 , pp. 85-91
    • Brennan, L.E.1    Nakagawa, J.2    Egger, D.3    Bienz, K.4    Moroni, C.5
  • 3
    • 0019017657 scopus 로고
    • The reversible dehydration of (R)-2-hydroxyglutarate to (E)-glutaconate
    • Buckel W (1980) The reversible dehydration of (R)-2-hydroxyglutarate to (E)-glutaconate. Eur J Biochem 106:439-447
    • (1980) Eur J Biochem , vol.106 , pp. 439-447
    • Buckel, W.1
  • 4
    • 0034788672 scopus 로고    scopus 로고
    • Unusual enzymes involved in five pathways of glutamate fermentation
    • Buckel W (2001) Unusual enzymes involved in five pathways of glutamate fermentation. Appl Microbiol Biotechnol 57:263-273
    • (2001) Appl Microbiol Biotechnol , vol.57 , pp. 263-273
    • Buckel, W.1
  • 5
    • 0028814950 scopus 로고
    • One electron redox reactions of CoASH esters in anaerobic bacteria. A mechanistic proposal
    • Buckel W, Keese R (1995) One electron redox reactions of CoASH esters in anaerobic bacteria. A mechanistic proposal. Angew Chem Int Edn Engl 34:1502-1506
    • (1995) Angew Chem Int Edn Engl , vol.34 , pp. 1502-1506
    • Buckel, W.1    Keese, R.2
  • 6
    • 0019401061 scopus 로고
    • Glutaconate CoA-transferase from Acidaminococcus fermentans
    • Buckel W, Dorn U, Semmler R (1981) Glutaconate CoA-transferase from Acidaminococcus fermentans. Eur J Biochem 118:315-321
    • (1981) Eur J Biochem , vol.118 , pp. 315-321
    • Buckel, W.1    Dorn, U.2    Semmler, R.3
  • 7
    • 4644280162 scopus 로고    scopus 로고
    • ATP-driven electron transfer in enzymatic radical reactions
    • Buckel W, Hetzel M, Kim J (2004) ATP-driven electron transfer in enzymatic radical reactions. Curr Opin Chem Biol 8:462-467
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 462-467
    • Buckel, W.1    Hetzel, M.2    Kim, J.3
  • 8
    • 0019980321 scopus 로고
    • Inherited 3-methylglutaconic aciduria in two brothers: Another defect of leucine metabolism
    • Duran M, Beemer FA, Tibosch AS, Bruinvis L, Ketting D, Wadman SK (1982) Inherited 3-methylglutaconic aciduria in two brothers: another defect of leucine metabolism. J Pediatr 101:551-554
    • (1982) J Pediatr , vol.101 , pp. 551-554
    • Duran, M.1    Beemer, F.A.2    Tibosch, A.S.3    Bruinvis, L.4    Ketting, D.5    Wadman, S.K.6
  • 9
    • 0035909051 scopus 로고    scopus 로고
    • Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli
    • Elssner T, Engemann C, Baumgart K, Kleber HP (2001) Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli. Biochemistry 40:11140-11148
    • (2001) Biochemistry , vol.40 , pp. 11140-11148
    • Elssner, T.1    Engemann, C.2    Baumgart, K.3    Kleber, H.P.4
  • 10
    • 0029791410 scopus 로고    scopus 로고
    • Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: A spiral fold defines the CoA-binding pocket
    • Engel CK, Mathieu M, Zeelen JP, Hiltunen JK, Wierenga RK (1996) Crystal structure of enoyl-coenzyme A (CoA) hydratase at 2.5 angstroms resolution: a spiral fold defines the CoA-binding pocket. EMBO J 15:5135-5145
    • (1996) EMBO J , vol.15 , pp. 5135-5145
    • Engel, C.K.1    Mathieu, M.2    Zeelen, J.P.3    Hiltunen, J.K.4    Wierenga, R.K.5
  • 12
    • 0024205873 scopus 로고
    • Assay of 3-methylglutaconyl-CoA hydratase
    • Gibson KM (1988) Assay of 3-methylglutaconyl-CoA hydratase. Methods Enzymol 166:214-218
    • (1988) Methods Enzymol , vol.166 , pp. 214-218
    • Gibson, K.M.1
  • 13
    • 0037035544 scopus 로고    scopus 로고
    • Adenosine triphosphate-induced electron transfer in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans
    • Hans M, Bill E, Cirpus I, Pierik AJ, Hetzel M, Alber D, Buckel W (2002) Adenosine triphosphate-induced electron transfer in 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. Biochemistry 41:5873-5882
    • (2002) Biochemistry , vol.41 , pp. 5873-5882
    • Hans, M.1    Bill, E.2    Cirpus, I.3    Pierik, A.J.4    Hetzel, M.5    Alber, D.6    Buckel, W.7
  • 14
    • 0012124314 scopus 로고
    • Methylglutaconase, eine neue Hydratase, die am Stoffwechsel verzweigter Carbonsäuren beteiligt ist
    • Hilz H, Knappe J, Ringelmann E, Lynen F (1958) Methylglutaconase, eine neue Hydratase, die am Stoffwechsel verzweigter Carbonsäuren beteiligt ist. Biochem Z 329:476-489
    • (1958) Biochem Z , vol.329 , pp. 476-489
    • Hilz, H.1    Knappe, J.2    Ringelmann, E.3    Lynen, F.4
  • 17
    • 33645968519 scopus 로고
    • Zur biochemischen Funktion des Biotins. I. Die Beteiligung der beta-methyl-crotonyl-carboxylase an der Bildung von beta-hydroxy-beta-methylglutaryl-CoA aus beta-hydroxy-isovaleryl-CoA
    • Knappe J, Schlegel H-G, Lynen F (1961) Zur biochemischen Funktion des Biotins. I. Die Beteiligung der beta-methyl-crotonyl-carboxylase an der Bildung von beta-hydroxy-beta-methylglutaryl-CoA aus beta-hydroxy-isovaleryl-CoA. Biochem Z 335:101-122
    • (1961) Biochem Z , vol.335 , pp. 101-122
    • Knappe, J.1    Schlegel, H.-G.2    Lynen, F.3
  • 19
    • 73049137089 scopus 로고
    • Zur biochemischen Funktion des Biotins. II. Reinigung und Wirkungsweise der beta-methyl-crotonyl-carboxylase
    • Lynen F, Knappe J, Lorch E, Jutting G, Ringelmann E, Lachance J-P (1961) Zur biochemischen Funktion des Biotins. II. Reinigung und Wirkungsweise der beta-methyl-crotonyl-carboxylase. Biochem Z 335:123-167
    • (1961) Biochem Z , vol.335 , pp. 123-167
    • Lynen, F.1    Knappe, J.2    Lorch, E.3    Jutting, G.4    Ringelmann, E.5    Lachance, J.-P.6
  • 20
    • 0028075976 scopus 로고
    • Location of the two genes encoding glutaconate coenzyme A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans
    • Mack M, Bendrat K, Zelder O, Eckel E, Linder D, Buckel W (1994) Location of the two genes encoding glutaconate coenzyme A-transferase at the beginning of the hydroxyglutarate operon in Acidaminococcus fermentans. Eur J Biochem 226:41-51
    • (1994) Eur J Biochem , vol.226 , pp. 41-51
    • Mack, M.1    Bendrat, K.2    Zelder, O.3    Eckel, E.4    Linder, D.5    Buckel, W.6
  • 21
    • 0016612419 scopus 로고
    • Substrate stereochemistry of the hydroxymethylglutraryl-CoA lyase and methylglutaconyl-CoA hydratase reactions
    • Messner B, Eggerer H, Cornforth JW, Mallaby R (1975) Substrate stereochemistry of the hydroxymethylglutraryl-CoA lyase and methylglutaconyl-CoA hydratase reactions. Eur J Biochem 53:255-264
    • (1975) Eur J Biochem , vol.53 , pp. 255-264
    • Messner, B.1    Eggerer, H.2    Cornforth, J.W.3    Mallaby, R.4
  • 22
    • 0000661488 scopus 로고
    • Protein degradation and proteolysis
    • Neidhardt FC, Ingraham JL, Brooks Low K, Magasanik B, Schaechter M, Umbarger HE (eds). American Society for Microbiology, Washington D. C
    • Miller CG (1987) Protein degradation and proteolysis. In: Neidhardt FC, Ingraham JL, Brooks Low K, Magasanik B, Schaechter M, Umbarger HE (eds) Escherichia coli and Salmonella typhimurium: cellular and molecular biology, vol 2. American Society for Microbiology, Washington D. C, pp 680-691
    • (1987) Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology , vol.2 , pp. 680-691
    • Miller, C.G.1
  • 26
    • 3543037565 scopus 로고    scopus 로고
    • Fungal metabolic model for type I 3-methylglutaconic aciduria
    • Rodriguez JM, Ruiz-Sala P, Ugarte M, Penalva MA (2004) Fungal metabolic model for type I 3-methylglutaconic aciduria. J Biol Chem 279:32385-32392
    • (2004) J Biol Chem , vol.279 , pp. 32385-32392
    • Rodriguez, J.M.1    Ruiz-Sala, P.2    Ugarte, M.3    Penalva, M.A.4
  • 33
    • 34250150693 scopus 로고
    • Studies on dissimilatory sulfate-reducing bacteria that decompose fatty acids. III. Characterization of the filamentous gliding Desulfonema limicola gen. nov. sp. nov., and Desulfonema magnum sp. nov.
    • Widdel F, Kohring GW, Mayer F (1983) Studies on dissimilatory sulfate-reducing bacteria that decompose fatty acids. III. Characterization of the filamentous gliding Desulfonema limicola gen. nov. sp. nov., and Desulfonema magnum sp. nov. Arch Microbiol 134:286-294
    • (1983) Arch Microbiol , vol.134 , pp. 286-294
    • Widdel, F.1    Kohring, G.W.2    Mayer, F.3
  • 34
    • 0025883684 scopus 로고
    • Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli
    • Yang XY, Schulz H, Elzinga M, Yang SY (1991) Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli. Biochemistry 30:6788-6795
    • (1991) Biochemistry , vol.30 , pp. 6788-6795
    • Yang, X.Y.1    Schulz, H.2    Elzinga, M.3    Yang, S.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.