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Volumn 272, Issue 3, 2005, Pages 813-821

Two beta-alanyl-CoA:ammonia lyases in Clostridium propionicum

Author keywords

Acryloyl CoA; Beta alanyl CoA; CoA transferase; L alanine and beta alanine fermentation; Pentamer

Indexed keywords

ACRYLOYL COENZYME A; ALANINE; AMMONIA; AMMONIA LYASE; AMMONIUM CHLORIDE; BACTERIAL ENZYME; BETA ALANINE; BETA ALANYL COENZYME A:AMMONIA LYASE; BETA AMINOBUTYRYL COENZYME A:AMMONIA LYASE; CARBON; COENZYME A; GENOMIC DNA; HYDRACRYLIC ACID; LACTIC ACID; LYSINE; THIOESTER; UNCLASSIFIED DRUG;

EID: 13444263419     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2004.04518.x     Document Type: Article
Times cited : (33)

References (37)
  • 1
    • 0000917545 scopus 로고
    • Fermentations of nitrogenous organic compounds
    • (Gunsalus IC, ed.). Academic Press Inc, New York
    • Barker HA (1961) Fermentations of nitrogenous organic compounds. In The Bacteria (Gunsalus IC, ed.), pp. 151-207. Academic Press Inc, New York.
    • (1961) The Bacteria , pp. 151-207
    • Barker, H.A.1
  • 2
    • 0018838186 scopus 로고
    • Beta-alanine synthesis in Escherichia coli
    • Cronan JE Jr (1980) Beta-alanine synthesis in Escherichia coli. J Bacterial 141, 1291-1297.
    • (1980) J Bacterial , vol.141 , pp. 1291-1297
    • Cronan Jr., J.E.1
  • 3
    • 0020003603 scopus 로고
    • Genetic and biochemical analyses of pantothenate biosynthesis in Escherichia coli and Salmonella typhimurium
    • Cronan JE Jr, Littel KJ & Jackowski S (1982) Genetic and biochemical analyses of pantothenate biosynthesis in Escherichia coli and Salmonella typhimurium. J Bacterial 149, 916-922.
    • (1982) J Bacterial , vol.149 , pp. 916-922
    • Cronan Jr., J.E.1    Littel, K.J.2    Jackowski, S.3
  • 5
    • 0028172783 scopus 로고
    • L-carnosine (beta-alanyl-L-histidine) and carcinine (beta- alanylhistamine) act as natural antioxidants with hydroxyl-radical-scavenging and lipid-peroxidase activities
    • Babizhayev MA, Seguin MC, Gueyne J, Evstigneeva RP, Ageyeva EA & Zheltukhina GA (1994) L-carnosine (beta-alanyl-L-histidine) and carcinine (beta-alanylhistamine) act as natural antioxidants with hydroxyl-radical- scavenging and lipid-peroxidase activities. Biochem J 304, 509-516.
    • (1994) Biochem J , vol.304 , pp. 509-516
    • Babizhayev, M.A.1    Seguin, M.C.2    Gueyne, J.3    Evstigneeva, R.P.4    Ageyeva, E.A.5    Zheltukhina, G.A.6
  • 6
    • 0026261761 scopus 로고
    • The biosynthetic origin of the pyridone ring of efrotomycin
    • Darland G, Arison B & Kaplan L (1991) The biosynthetic origin of the pyridone ring of efrotomycin. J Ind Microbiol 8, 265-271.
    • (1991) J Ind Microbiol , vol.8 , pp. 265-271
    • Darland, G.1    Arison, B.2    Kaplan, L.3
  • 7
    • 0034523714 scopus 로고    scopus 로고
    • Production of cyclodepsipeptides destruxin A and B from Metarhizium anisopliae
    • Liu BL, Chen JW & Tzeng YM (2000) Production of cyclodepsipeptides destruxin A and B from Metarhizium anisopliae. Biotechnol Prog 16, 993-999.
    • (2000) Biotechnol Prog , vol.16 , pp. 993-999
    • Liu, B.L.1    Chen, J.W.2    Tzeng, Y.M.3
  • 8
    • 13444262795 scopus 로고
    • Propionic acid metabolism. 5. The conversion of beta-alanine to propionic acid by cellfree extracts of Clostridium propioncum
    • Goldfine H & Stadtman ER (1960) Propionic acid metabolism. 5. The conversion of beta-alanine to propionic acid by cellfree extracts of Clostridium propioncum. J Biol Chem 235, 2238-2245.
    • (1960) J Biol Chem , vol.235 , pp. 2238-2245
    • Goldfine, H.1    Stadtman, E.R.2
  • 9
    • 0017343370 scopus 로고
    • Energy conservation in chemotrophic anaerobic bacteria
    • Thauer RK, Jungermann K & Decker K (1977) Energy conservation in chemotrophic anaerobic bacteria. Bacterial Rev 41, 100-180.
    • (1977) Bacterial Rev , vol.41 , pp. 100-180
    • Thauer, R.K.1    Jungermann, K.2    Decker, K.3
  • 10
    • 0000968840 scopus 로고
    • Two new amino-acid-fermenting bacteria, Clostridium propionicum and Diplococcus glycinophilus
    • Cardon BP & Barker HA (1946) Two new amino-acid-fermenting bacteria, Clostridium propionicum and Diplococcus glycinophilus. J Bacteriol 52, 629-634.
    • (1946) J Bacteriol , vol.52 , pp. 629-634
    • Cardon, B.P.1    Barker, H.A.2
  • 11
    • 0001485428 scopus 로고
    • Amino acid fermentations by Clostridium propionicum and Diplococcus glycinophilus
    • Cardon BP & Barker HA (1947) Amino acid fermentations by Clostridium propionicum and Diplococcus glycinophilus. Arch Biochem Biophys 12, 165-171.
    • (1947) Arch Biochem Biophys , vol.12 , pp. 165-171
    • Cardon, B.P.1    Barker, H.A.2
  • 12
    • 8244237034 scopus 로고
    • The mechanism of propionic acid formation by Clostridium propionicum
    • Johns AT (1952) The mechanism of propionic acid formation by Clostridium propionicum. J General Microbiol 6, 123-127.
    • (1952) J General Microbiol , vol.6 , pp. 123-127
    • Johns, A.T.1
  • 13
    • 0013639102 scopus 로고
    • The fermentation of three carbon substrates by Clostridium propionicum and Propionibacterium
    • Leaver FW, Wood HG & Stjernholm R (1955) The fermentation of three carbon substrates by Clostridium propionicum and Propionibacterium. J Bacterial 70, 521-530.
    • (1955) J Bacterial , vol.70 , pp. 521-530
    • Leaver, F.W.1    Wood, H.G.2    Stjernholm, R.3
  • 14
    • 0021755004 scopus 로고
    • On the dehydration of (R)-lactate in the fermentation of alanine to propionate by Clostridium propionicum
    • Schweiger G & Buckel W (1984) On the dehydration of (R)-lactate in the fermentation of alanine to propionate by Clostridium propionicum. FEBS Lett 171, 79-84.
    • (1984) FEBS Lett , vol.171 , pp. 79-84
    • Schweiger, G.1    Buckel, W.2
  • 15
    • 0021795694 scopus 로고
    • Identification of aerylate, the product of the dehydration of (R)-lactate catalysed by cell-free extracts from Clostridium propionicum
    • Schweiger G & Buckel W (1985) Identification of aerylate, the product of the dehydration of (R)-lactate catalysed by cell-free extracts from Clostridium propionicum. FEBS Lett 185, 253-256.
    • (1985) FEBS Lett , vol.185 , pp. 253-256
    • Schweiger, G.1    Buckel, W.2
  • 16
    • 0036151093 scopus 로고    scopus 로고
    • Propionate CoA-transferase from Clostridium propionicum. Cloning of gene and identification of glutamate 324 at the active site
    • Selmer T, Willanzheimer A & Hetzel M (2002) Propionate CoA-transferase from Clostridium propionicum. Cloning of gene and identification of glutamate 324 at the active site. Eur J Biochem 269, 372-380.
    • (2002) Eur J Biochem , vol.269 , pp. 372-380
    • Selmer, T.1    Willanzheimer, A.2    Hetzel, M.3
  • 17
    • 0037338481 scopus 로고    scopus 로고
    • Acryloyl-CoA reductase from Clostridium propionicum. An enzyme complex of propionyl-CoA dehydrogenase and electron-transferring flavoprotein
    • Hetzel M, Brock M, Selmer T, Pierik AJ, Golding BT & Buckel W (2003) Acryloyl-CoA reductase from Clostridium propionicum. An enzyme complex of propionyl-CoA dehydrogenase and electron-transferring flavoprotein. Eur J Biochem 270, 902-910.
    • (2003) Eur J Biochem , vol.270 , pp. 902-910
    • Hetzel, M.1    Brock, M.2    Selmer, T.3    Pierik, A.J.4    Golding, B.T.5    Buckel, W.6
  • 19
    • 0003942010 scopus 로고
    • Propionic acid metabolism. I. The purification and properties of acrylyl coenzyme A aminase
    • Vagelos PR, Earl JM & Stadtman ER (1959) Propionic acid metabolism. I. The purification and properties of acrylyl coenzyme A aminase. J Biol Chem 234, 490-497.
    • (1959) J Biol Chem , vol.234 , pp. 490-497
    • Vagelos, P.R.1    Earl, J.M.2    Stadtman, E.R.3
  • 24
    • 0031029502 scopus 로고    scopus 로고
    • Identification and classification of Oxalobacter formigenes strains by using oligonucleotide probes and primers
    • Sidhu H, Allison M & Peck AB (1997) Identification and classification of Oxalobacter formigenes strains by using oligonucleotide probes and primers. J Clin Microbiol 35, 350-353.
    • (1997) J Clin Microbiol , vol.35 , pp. 350-353
    • Sidhu, H.1    Allison, M.2    Peck, A.B.3
  • 26
    • 0023217214 scopus 로고
    • Equilibrium constants of several reactions involved in the fermentation of glutamate
    • Buckel W & Miller SL (1987) Equilibrium constants of several reactions involved in the fermentation of glutamate. Eur J Biochem 164, 565-569.
    • (1987) Eur J Biochem , vol.164 , pp. 565-569
    • Buckel, W.1    Miller, S.L.2
  • 27
    • 0035861886 scopus 로고    scopus 로고
    • A new family of CoA-transferases
    • Heider J (2001) A new family of CoA-transferases. FEBS Lett 509, 345-349.
    • (2001) FEBS Lett , vol.509 , pp. 345-349
    • Heider, J.1
  • 28
    • 0009747709 scopus 로고
    • Fermentative processes of the fusiform bacteria
    • Jackins HC & Barker HA (1951) Fermentative processes of the fusiform bacteria. J Bacteriol 61, 101-114.
    • (1951) J Bacteriol , vol.61 , pp. 101-114
    • Jackins, H.C.1    Barker, H.A.2
  • 29
    • 0020359798 scopus 로고
    • Pathway of lysine degradation in Fusobacterium nucleatum
    • Barker HA, Kahn JM & Hedrick L (1982) Pathway of lysine degradation in Fusobacterium nucleatum. J Bacteriol 152, 201-207.
    • (1982) J Bacteriol , vol.152 , pp. 201-207
    • Barker, H.A.1    Kahn, J.M.2    Hedrick, L.3
  • 30
    • 0016303903 scopus 로고
    • Purification and properties of L-3-aminobutyryl coenzyme A deaminase from a lysine-fermenting Clostridium
    • Jeng IM & Barker HA (1974) Purification and properties of L-3-aminobutyryl coenzyme A deaminase from a lysine-fermenting Clostridium. J Biol Chem 249, 6578-6584.
    • (1974) J Biol Chem , vol.249 , pp. 6578-6584
    • Jeng, I.M.1    Barker, H.A.2
  • 31
    • 13444273815 scopus 로고    scopus 로고
    • (2004) 3-Hydroxypropionic acid and other organic compounds. US Patent Application 20040076982, Cargill Incorporated, Minneapolis, MN, USA
    • Gokarn RR, Selifonova OV, Jessen HJ, Gort SJ, Seimer T & Buckel W (2004) 3-Hydroxypropionic acid and other organic compounds. US Patent Application 20040076982, Cargill Incorporated, Minneapolis, MN, USA.
    • Gokarn, R.R.1    Selifonova, O.V.2    Jessen, H.J.3    Gort, S.J.4    Seimer, T.5    Buckel, W.6
  • 32
    • 0037122939 scopus 로고    scopus 로고
    • Fumarate respiration of Wolinella succinogenes: Enzymology, energetics and coupling mechanism
    • Kröger A, Biel S, Simon J, Gross R, Unden G & Lancaster CR (2002) Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism. Biochim Biophys Acta 1553, 23-38.
    • (2002) Biochim Biophys Acta , vol.1553 , pp. 23-38
    • Kröger, A.1    Biel, S.2    Simon, J.3    Gross, R.4    Unden, G.5    Lancaster, C.R.6
  • 33
    • 2242471038 scopus 로고    scopus 로고
    • Energetics and kinetics of lactate fermentation to acetate and propionate via methylmalonyl-CoA or acrylyl-CoA
    • Seeliger S, Janssen PH & Schink B (2002) Energetics and kinetics of lactate fermentation to acetate and propionate via methylmalonyl-CoA or acrylyl-CoA. FEMS Microbiol Lett 211, 65-70.
    • (2002) FEMS Microbiol Lett , vol.211 , pp. 65-70
    • Seeliger, S.1    Janssen, P.H.2    Schink, B.3
  • 34
    • 0000060558 scopus 로고
    • The preparation of 5-succinyl-coenzyme A
    • Simon E & Shemin D (1953) The preparation of 5-succinyl-coenzyme A. J Am Chem Soc 75, 2520.
    • (1953) J Am Chem Soc , vol.75 , pp. 2520
    • Simon, E.1    Shemin, D.2
  • 35
    • 0033597932 scopus 로고    scopus 로고
    • Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentons. Implications for the mechanism of CoA-ester hydrolysis
    • Seimer T & Buckel W (1999) Oxygen exchange between acetate and the catalytic glutamate residue in glutaconate CoA-transferase from Acidaminococcus fermentons. Implications for the mechanism of CoA-ester hydrolysis. J Biol Chem 274, 20772-20778.
    • (1999) J Biol Chem , vol.274 , pp. 20772-20778
    • Seimer, T.1    Buckel, W.2
  • 36
    • 0029130352 scopus 로고
    • A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency
    • Schmidt B, Seimer T, Ingendoh A & von Figura K (1995) A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell 82, 271-278.
    • (1995) Cell , vol.82 , pp. 271-278
    • Schmidt, B.1    Seimer, T.2    Ingendoh, A.3    Von Figura, K.4
  • 37
    • 0017886452 scopus 로고
    • The redox potential of dithionite and SO-2 from equilibrium reactions with flavodoxins, methyl, viologen and hydrogen plus hydrogenase
    • Mayhew SG (1978) The redox potential of dithionite and SO-2 from equilibrium reactions with flavodoxins, methyl, viologen and hydrogen plus hydrogenase. Eur J Biochem 85, 535-547.
    • (1978) Eur J Biochem , vol.85 , pp. 535-547
    • Mayhew, S.G.1


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