Purification and characterization of flavokinase from Neurospora crassa.
Indian J Biochem Biophys
;
1999 Jun; 36(3): 137-42
Article
Dans Anglais
| IMSEAR
| ID: sea-27520
ABSTRACT
The ATP-dependent phosphorylation of riboflavin to FMN by flavokinase is the key step in flavin biosynthesis. Flavokinase has been purified from a fungal source for the first time. The enzyme purified from a cell wall lacking mutant of Neurospora crassa, slime, is a monomer of M(r) 35.5 kDa with maximal activity at alkaline pH and high temperature (55 degrees C). The K(m) for both substrates is the lowest reported for flavokinase from any source so far (120 nM for riboflavin and 210 nM for MgATP2-). The enzyme exhibits preference for Mg2+ over Zn2+ as the essential activator and is also significantly activated by several cations. Activation by orthophosphate may be physiologically relevant for the intracellular regulation of flavokinase.
Texte intégral:
Disponible
Indice:
IMSEAR (Asie du Sud-Est)
Sujet Principal:
Cinétique
/
Phosphotransferases (Alcohol Group Acceptor)
/
Température élevée
/
Concentration en ions d'hydrogène
/
Masse moléculaire
/
Neurospora crassa
langue:
Anglais
Texte intégral:
Indian J Biochem Biophys
Année:
1999
Type:
Article
Documents relatifs à ce sujet
MEDLINE
...
LILACS
LIS