Αναγραμματισμοί & Πληροφορίες σχετικά με | Αγγλικά λέξη ACETOIN


ACETOIN

6

Αριθμός γραμμάτων

7

Είναι το παλτοδρόμιο

Όχι

12
AC
ACE
CE
CET
ET
ETO
IN
OI
TO
TOI

1

1

463
AC
ACE
ACI
ACN
ACT

Παραδείγματα χρήσης ACETOIN σε μια πρόταση

  • Together with the acetylpolyamine amidohydrolases and the acetoin utilization proteins, the histone deacetylases form an ancient protein superfamily known as the histone deacetylase superfamily.
  • The conversion of acetoin into acetyl-CoA is catalysed by the acetoin dehydrogenase complex, following a mechanism largely analogous to the pyruvate dehydrogenase complex; however, as acetoin is not a 2-oxoacid, it does not undergo decarboxylation by the E1 enzyme; instead, a molecule of acetaldehyde is released.
  • It also tests positive for acetoin production, arginine, dihydrolase, benzidine, catalase, hemolysis, and lipase; it tests negative for coagulase, DNase, ornithine decarboxylase and phosphatase.
  • Other names in common use include butyleneglycol dehydrogenase, D-butanediol dehydrogenase, D-(−)-butanediol dehydrogenase, butylene glycol dehydrogenase, diacetyl (acetoin) reductase, D-aminopropanol dehydrogenase, D-aminopropanol dehydrogenase, 1-amino-2-propanol dehydrogenase, 2,3-butanediol dehydrogenase, D-1-amino-2-propanol dehydrogenase, (R)-diacetyl reductase, (R)-2,3-butanediol dehydrogenase, D-1-amino-2-propanol:NAD oxidoreductase, 1-amino-2-propanol oxidoreductase, and aminopropanol oxidoreductase.
  • The majority of Streptococcus anginosus strains produce acetoin from glucose, ferment lactose, trehalose, salicin, and sucrose, and hydrolyze esculin and arginine.
  • It is negative for clumping factor, coagulase, hyaluronidase, arginine dihydrolase, ornithine decarboxylase, acetoin, arginine arylamidase, alpha- and beta-haemolysins, heat-stable and heat-labile nucleases, indole, hydrogen sulphide, and lecithinase.
  • In the presence of atmospheric oxygen and 40% KOH, acetoin is converted to diacetyl and α-naphthol serves as catalyst to bring out red color complex.



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