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Adenosylmethionine-8-amino-7-oxononanoate transaminase

Part of the Springer Handbook of Enzymes book series (HDBKENZYMES, volume 35)

Nomenclature

EC number

2.6.1.62

Systematic name

S-adenosyl-l-methionine:8-amino-7-oxononanoate aminotransferase

Recommended name

adenosylmethionine-8-amino-7-oxononanoate transaminase

Synonyms

7,8-diaminononanoate transaminase

7,8-diaminopelargonic acid aminotransferase

7-keto-8-aminopelargonic acid aminotransferase

7-keto-8-aminopelargonic acid-7,8-diaminopelargonic acid aminotransferase

DAPA aminotransferase

DAPA synthase

DAPA transaminase

diaminopelargonate synthase

synthase, diaminopelargonate

CAS registry number

37259-71-5

Keywords

Escherichia Coli Molecular Weight Crystal Structure Cancer Research Veterinary Medicine 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. [1]
    Stoner, G.L.; Eisenberg, M.A.: Purification and properties of 7,8-diaminopelargonic acid aminotransferase. J. Biol. Chem., 250, 4029–4036 (1975)PubMedGoogle Scholar
  2. [2]
    Izumi, Y.; Sato, K.; Tani, Y.; Ogata, K.: Purification and properties of 7,8-diaminopelargonic acid aminotransferase. Agric. Biol. Chem., 39, 175–181 (1975)Google Scholar
  3. [3]
    Izumi, Y.; Sato, K.; Tani, Y.; Ogata, K.: 7,8-Diaminopelargonic acid aminotransferase, an enzyme involved in biotin biosynthesis by microorganisms. Agric. Biol. Chem., 37, 2683–2684 (1973)Google Scholar
  4. [4]
    Stoner, G.L.; Eisenberg, M.A.: Biosynthesis of 7,8-diaminopelargonic acid from 7-keto-8-aminopelargonic acid and S-adenosyl-l-methionine. The kinetics of the reaction. J. Biol. Chem., 250, 4037–4043 (1975)PubMedGoogle Scholar
  5. [5]
    Izumi, Y.; Tani, Y.; Ogata, K.: Microbiological biosynthesis of biotin. Methods Enzymol., 62, 326–338 (1979)PubMedGoogle Scholar
  6. [6]
    Eisenberg, M.A.; Stoner, G.L.: 7,8-Diaminopelargonic acid aminotransferase. Methods Enzymol., 62, 342–347 (1979)PubMedCrossRefGoogle Scholar
  7. [7]
    Eliot, A.C.; Sandmark, J.; Schneider, G.; Kirsch, J.F.: The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation. Biochemistry, 41, 12582–12589 (2002)PubMedCrossRefGoogle Scholar
  8. [8]
    Käck, H.; Gibson, K.J.; Gatenby, A.A.; Schneider, G.; Lindqvist, Y.: Purification and preliminary x-ray crystallographic studies of recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli. Acta Crystallogr. Sect. D, D54, 1397–1398 (1998)CrossRefGoogle Scholar
  9. [9]
    Käck, H.; Sandmark, J.; Gibson, K.; Schneider, G.; Lindqvist, Y.: Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5′-phosphate-dependent enzymes. J. Mol. Biol., 291, 857–876 (1999)PubMedCrossRefGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2007

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