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Volumn 236, Issue 1, 1996, Pages 301-308

Mechanistic studies on the 8-amino-7-oxopelargonate synthase, a pyridoxal-5'-phosphate-dependent enzyme involved in biotin biosynthesis

(2)  Ploux, O a   Marquet, A a  

a CNRS   (France)

Author keywords

8 amino 7 oxopelargonate synthase; Biotin biosynthesis; Isotope exchange reaction; Pyridoxal 5' phosphate; Reaction mechanism

Indexed keywords

8 AMINO 7 OXOPELARGONATE SYNTHETASE; BIOTIN; SYNTHETASE; UNCLASSIFIED DRUG;

EID: 0029981540     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.00301.x     Document Type: Article
Times cited : (43)

References (37)
  • 1
    • 0014348406 scopus 로고
    • Synthesis of 7‐oxo‐8‐aminopel‐argonic acid, a biotin vitamer, in cell‐free extracts of Escherichia coli biotin auxotrophs
    • 1 Eisenberg, M. A. & Star, C. (1968) Synthesis of 7‐oxo‐8‐aminopel‐argonic acid, a biotin vitamer, in cell‐free extracts of Escherichia coli biotin auxotrophs, J. Bacteriol. 96, 1291–1297.
    • (1968) J. Bacteriol. , vol.96 , pp. 1291-1297
    • Eisenberg, M.A.1    Star, C.2
  • 2
    • 0015908459 scopus 로고
    • Partial purification and some properties of 7‐keto‐8‐aminopelargonic acid synthetase, an enzyme involved in biotin biosynthesis
    • 2 Izumi, Y., Morita, H., Tani, Y. & Ogata, K. (1973) Partial purification and some properties of 7‐keto‐8‐aminopelargonic acid synthetase, an enzyme involved in biotin biosynthesis, Agric. Biol. Chem. 37, 1327–1333.
    • (1973) Agric. Biol. Chem. , vol.37 , pp. 1327-1333
    • Izumi, Y.1    Morita, H.2    Tani, Y.3    Ogata, K.4
  • 3
    • 0015886708 scopus 로고
    • Distribution of 7‐keto‐8‐aininopelargonic acid synthetase in bacteria and the control mechanism of the enzyme activity
    • 3 Izumi, Y., Sato, K., Tani, Y. & Ogata, K. (1973) Distribution of 7‐keto‐8‐aininopelargonic acid synthetase in bacteria and the control mechanism of the enzyme activity, Agric. Biol. Chem. 37, 1335–1340.
    • (1973) Agric. Biol. Chem. , vol.37 , pp. 1335-1340
    • Izumi, Y.1    Sato, K.2    Tani, Y.3    Ogata, K.4
  • 4
    • 0026603151 scopus 로고
    • The 8‐amino‐7‐oxopelargonate synthase from Bacillus sphaericus
    • 4 Ploux, O. & Marquet, A. (1992) The 8‐amino‐7‐oxopelargonate synthase from Bacillus sphaericus, Biochem. J. 283, 327–331.
    • (1992) Biochem. J. , vol.283 , pp. 327-331
    • Ploux, O.1    Marquet, A.2
  • 5
    • 77956929400 scopus 로고
    • δ‐Aminolevulinic acid synthetase, in: The enzymes
    • 5 Jordan, P. M. & Shemin, D. (1972) δ‐Aminolevulinic acid synthetase, in The enzymes ( Boyer, P. D., ed.) 3rd edn, vol. 7, pp. 339–356, Academic Press, New York.
    • (1972) , vol.7 , pp. 339-356
    • Jordan, P.M.1    Shemin, D.2
  • 6
    • 0021333971 scopus 로고
    • Enzymology of long‐chain base synthesis by liver: characterization of serine palmitoyltransferase in rat liver microsomes
    • 6 Williams, R. D., Wang, E. & Merrill, A. H. Jr (1984) Enzymology of long‐chain base synthesis by liver: characterization of serine palmitoyltransferase in rat liver microsomes, Arch. Biochem. Biophys. 228, 282–291.
    • (1984) Arch. Biochem. Biophys. , vol.228 , pp. 282-291
    • Williams, R.D.1    Wang, E.2    Merrill, A.H.3
  • 7
    • 0023665217 scopus 로고
    • Purification, properties and N‐terminal amino acid sequence of homogeneous Escherichia coli 2‐amino‐3‐ketobutyrate CoA ligase, a pyridoxal phonphate‐dependent enzyme
    • 7 Mukherjee, J. J. & Dekker, E. E. (1987) Purification, properties and N‐terminal amino acid sequence of homogeneous Escherichia coli 2‐amino‐3‐ketobutyrate CoA ligase, a pyridoxal phonphate‐dependent enzyme, J. Biol. Chem. 262, 14441–14447.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14441-14447
    • Mukherjee, J.J.1    Dekker, E.E.2
  • 8
    • 0023075669 scopus 로고
    • Structure of the Bradyrhizobium japonicum gene hemA encoding 5‐aminolevulinic acid synthase
    • 8 McClung, C. R., Somerville, J. E., Guerinot, M. L. & Chelm, B. K. (1987) Structure of the Bradyrhizobium japonicum gene hemA encoding 5‐aminolevulinic acid synthase, Gene 54, 133–139.
    • (1987) Gene , vol.54 , pp. 133-139
    • McClung, C.R.1    Somerville, J.E.2    Guerinot, M.L.3    Chelm, B.K.4
  • 9
    • 0024296603 scopus 로고
    • Nucleotide sequence of the 2‐amino‐3‐ketoburyrate coenzyme A ligase (kbl) gene of E. coli
    • 9 Aronson, B. D., Ravnikar, P. D. & Somerville, R. L. (1988) Nucleotide sequence of the 2‐amino‐3‐ketoburyrate coenzyme A ligase (kbl) gene of E. coli, Nucleic Acids Res. 16, 3586.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 3586
    • Aronson, B.D.1    Ravnikar, P.D.2    Somerville, R.L.3
  • 11
    • 0025342768 scopus 로고
    • Cloning and characterization of the Bacillus sphaericus genes controlling the bioconversion of pimelate into dethiobiotin
    • 11 Gloeckler, R., Ohsawa, I., Speck, D., Ledoux, C., Bernard, S., Zinsius, M., Villeval, D., Kisou, T., Kamogawa, K. & Lemoine, Y. (1990) Cloning and characterization of the Bacillus sphaericus genes controlling the bioconversion of pimelate into dethiobiotin, Gene 87, 63–70.
    • (1990) Gene , vol.87 , pp. 63-70
    • Gloeckler, R.1    Ohsawa, I.2    Speck, D.3    Ledoux, C.4    Bernard, S.5    Zinsius, M.6    Villeval, D.7    Kisou, T.8    Kamogawa, K.9    Lemoine, Y.10
  • 12
    • 0025739993 scopus 로고
    • Cloning and characterization of LCB1, a Saccharomyces gene required for biosynthesis of the long‐chain base component of sphingolipids
    • 12 Buede, R., Rinker‐Schaffer, C., Pinto, W. J., Lester, R. L. & Dickson, R. C. (1991) Cloning and characterization of LCB1, a Saccharomyces gene required for biosynthesis of the long‐chain base component of sphingolipids, J. Bacteriol. 173, 4325–4332.
    • (1991) J. Bacteriol. , vol.173 , pp. 4325-4332
    • Buede, R.1    Rinker‐Schaffer, C.2    Pinto, W.J.3    Lester, R.L.4    Dickson, R.C.5
  • 13
    • 0017298744 scopus 로고
    • Mechanism and stereochemistry of enzymic reactions involved in porphyrin biosynthesis
    • 13 Akhtar, M., Abboud, M. M., Barnard, G., Jordan, P. & Zaman, Z. (1976) Mechanism and stereochemistry of enzymic reactions involved in porphyrin biosynthesis, Phil. Trans. R. Soc. Lond. B. 273, 117–136.
    • (1976) Phil. Trans. R. Soc. Lond. B. , vol.273 , pp. 117-136
    • Akhtar, M.1    Abboud, M.M.2    Barnard, G.3    Jordan, P.4    Zaman, Z.5
  • 14
    • 0017353099 scopus 로고
    • An exchange reaction catalysed by δ‐aminolaevulinate synthase from Rhodopseudomonas spheroides
    • 14 Laghai, A. & Jordan, P. M. (1977) An exchange reaction catalysed by δ‐aminolaevulinate synthase from Rhodopseudomonas spheroides, Biochem. Soc. Trans. 5, 299–300.
    • (1977) Biochem. Soc. Trans. , vol.5 , pp. 299-300
    • Laghai, A.1    Jordan, P.M.2
  • 15
    • 0017255320 scopus 로고
    • A partial reaction of δ‐aminolae‐vulinate synthetase from Rhodopseudomonas spheroides
    • 15 Laghai, A. & Jordan, P. M. (1976) A partial reaction of δ‐aminolae‐vulinate synthetase from Rhodopseudomonas spheroides, Biochem. Soc. Trans. 4, 52.
    • (1976) Biochem. Soc. Trans. , vol.4 , pp. 52
    • Laghai, A.1    Jordan, P.M.2
  • 16
    • 37049136992 scopus 로고
    • Biosynthesis of 5‐aminolevulinic acid: involvement of a retention‐inversion mechanism
    • 16 Abboud, M. M., Jordan, P. M. & Akhtar, M. (1974) Biosynthesis of 5‐aminolevulinic acid: involvement of a retention‐inversion mechanism, J. Chem. Soc. Chem. Commun., 643–644.
    • (1974) J. Chem. Soc. Chem. Commun. , pp. 643-644
    • Abboud, M.M.1    Jordan, P.M.2    Akhtar, M.3
  • 17
    • 0015889955 scopus 로고
    • Mechanism and stereochemistry of the 5‐aminolaevulinate synthetase reaction
    • 17 Zaman, Z., Jordan, P. M. & Akhtar, M. (1973) Mechanism and stereochemistry of the 5‐aminolaevulinate synthetase reaction, Biochem. J. 135, 257–263.
    • (1973) Biochem. J. , vol.135 , pp. 257-263
    • Zaman, Z.1    Jordan, P.M.2    Akhtar, M.3
  • 18
    • 0344648865 scopus 로고
    • The mechanism of the action of δ‐aminolaevulate synthetase and the synthesis of stereospecifically tritiated glycine
    • 18 Akhtar, M. & Jordan, P. M. (1968), The mechanism of the action of δ‐aminolaevulate synthetase and the synthesis of stereospecifically tritiated glycine, J. Chem. Soc. Chem. Commun., 1691–1692.
    • (1968) J. Chem. Soc. Chem. Commun. , pp. 1691-1692
    • Akhtar, M.1    Jordan, P.M.2
  • 19
    • 0018241826 scopus 로고
    • Studies on δ‐aminolevulinic acid synthase of Rhodopseudomonas spheroides
    • 19 Nandi, D. L. (1978) Studies on δ‐aminolevulinic acid synthase of Rhodopseudomonas spheroides, J. Biol. Chem. 253, 8872–8877.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8872-8877
    • Nandi, D.L.1
  • 20
    • 0038273218 scopus 로고
    • The biosynthesis of sphingosine
    • 20 Weiss, B. (1963) The biosynthesis of sphingosine, J. Biol. Chem. 238, 1953–1959.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1953-1959
    • Weiss, B.1
  • 21
    • 0017233388 scopus 로고
    • Studies on the mechanism of 3‐ketosphinganine synthetase
    • 21 Krisnangkura, K. & Sweeley, C. C. (1976) Studies on the mechanism of 3‐ketosphinganine synthetase, J. Biol. Chem. 251, 1597–1602.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1597-1602
    • Krisnangkura, K.1    Sweeley, C.C.2
  • 23
    • 0004136246 scopus 로고
    • Molecular cloning: a laboratory manual
    • 23 Sambrook, J., Fritsch, E. F. & Maniatis, T. (1989) Molecular cloning: a laboratory manual, 2nd edn, Cold Spring Harbor Laboratory, Cold Spring Harbor NY.
    • (1989)
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 24
    • 0017782201 scopus 로고
    • A general method for the preparation of α‐labeled amino acids
    • 24 Upson, D. A. & Hruby, V. J. (1977) A general method for the preparation of α‐labeled amino acids, J. Org. Chem. 42, 2329–2330.
    • (1977) J. Org. Chem. , vol.42 , pp. 2329-2330
    • Upson, D.A.1    Hruby, V.J.2
  • 25
    • 0003828322 scopus 로고
    • Chemistry of the amino acids
    • 25 Greenstein, J. P. & Winitz, M. (1961) Chemistry of the amino acids, vol. 3, pp. 1819–1840, John Wiley & Sons, New York.
    • (1961) , vol.3 , pp. 1819-1840
    • Greenstein, J.P.1    Winitz, M.2
  • 26
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein‐dye binding
    • 26 Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein‐dye binding, Anal. Biochem. 72, 248–254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 27
    • 0003443846 scopus 로고
    • Methods in enzymatic analysis
    • 27 Bergmeyer, H. U. (1983) Methods in enzymatic analysis, 3rd edn, VCH, Weinheim.
    • (1983)
    • Bergmeyer, H.U.1
  • 29
    • 0026441346 scopus 로고
    • Investigation of the first step of biotin biosynthesis in Bacillus sphaericus
    • 29 Ploux, O., Soularue, P., Marquet, A., Gloeckler, R. & Lemoine, Y. (1992) Investigation of the first step of biotin biosynthesis in Bacillus sphaericus, Biochem. J. 287, 685–690.
    • (1992) Biochem. J. , vol.287 , pp. 685-690
    • Ploux, O.1    Soularue, P.2    Marquet, A.3    Gloeckler, R.4    Lemoine, Y.5
  • 30
    • 0003408336 scopus 로고
    • Catalysis in Chemistry and enzymology
    • 30 Jencks, W. P. (1987) Catalysis in Chemistry and enzymology, 2nd edn, pp. 276–277, Dover Publication, New York.
    • (1987) , pp. 276-277
    • Jencks, W.P.1
  • 31
    • 0024282743 scopus 로고
    • Isotope effect studies of the pyridoxal 5′‐phosphate dependent histidine decarboxylase from Morganella morganii
    • 31 Abell, L. M. & O'Leary, M. H. (1988) Isotope effect studies of the pyridoxal 5′‐phosphate dependent histidine decarboxylase from Morganella morganii, Biochemistry 27, 5927–5933.
    • (1988) Biochemistry , vol.27 , pp. 5927-5933
    • Abell, L.M.1    O'Leary, M.H.2
  • 32
    • 0023783635 scopus 로고
    • Isotope effect studies of the pyruvate‐dependent histidine decarboxylase from Lactobacillus 30 a
    • 32 Abell, L. M. & O'Leary, M. H. (1988) Isotope effect studies of the pyruvate‐dependent histidine decarboxylase from Lactobacillus 30 a, Biochemistry 27, 5933–5939.
    • (1988) Biochemistry , vol.27 , pp. 5933-5939
    • Abell, L.M.1    O'Leary, M.H.2
  • 33
    • 0016136725 scopus 로고
    • D2O‐Alanine exchange reactions catalyzed by alanine racemase and glutamic pyruvic transaminase
    • 33 Babu, U. M. & Johnston, R. B. (1974) D 2 O‐Alanine exchange reactions catalyzed by alanine racemase and glutamic pyruvic transaminase, Biochem. Biophys. Res. Commun. 58, 460–466.
    • (1974) Biochem. Biophys. Res. Commun. , vol.58 , pp. 460-466
    • Babu, U.M.1    Johnston, R.B.2
  • 34
    • 0017280657 scopus 로고
    • Proton magnetic resonance studies of glutamate‐alanine transaminase‐catalyzed deuterium exchange
    • 34 Cooper, A. J. L. (1976) Proton magnetic resonance studies of glutamate‐alanine transaminase‐catalyzed deuterium exchange, J. Biol. Chem. 251, 1088–1096.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1088-1096
    • Cooper, A.J.L.1
  • 35
    • 0017626307 scopus 로고
    • The effects of pH on the rates of isotope exchange catalyzed by alanine aminotransferase
    • 35 Golichowski, A., Harruff, R. C. & Jenkins, W. T. (1977) The effects of pH on the rates of isotope exchange catalyzed by alanine aminotransferase, Arch. Biochem. Biophys. 178, 459–467.
    • (1977) Arch. Biochem. Biophys. , vol.178 , pp. 459-467
    • Golichowski, A.1    Harruff, R.C.2    Jenkins, W.T.3
  • 36
    • 0542407520 scopus 로고
    • Pyridoxal phosphate enzymes catalyzing racemization, in: Vitamin B6 pyridoxal phosphate
    • 36 Soda, K., Tanaka, H. & Tanizawa, K. (1986) Pyridoxal phosphate enzymes catalyzing racemization, in Vitamin B6 pyridoxal phosphate ( Dolphin, D., Poulson, R. & Avramovic, O., eds) part B, pp. 223–251, John Wiley & Sons, New York.
    • (1986) , pp. 223-251
    • Soda, K.1    Tanaka, H.2    Tanizawa, K.3
  • 37
    • 33748670843 scopus 로고
    • Stereochemistry of pyridoxal phosphate‐catalyzed reactions. in New comprehensive biochemistry, vol. 3, in: Stereochemistry
    • 37 Floss, H. G. & Vederas, J. C. (1982) Stereochemistry of pyridoxal phosphate‐catalyzed reactions. in New comprehensive biochemistry, vol. 3, Stereochemistry ( Tamm, C., ed.) pp. 161–199. Elsevier Biomedical Press, Amsterdam.
    • (1982) , pp. 161-199
    • Floss, H.G.1    Vederas, J.C.2


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