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<span style="font-size:12.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-ansi-language: EN-IN;mso-fareast-language:EN-IN;mso-bidi-language:AR-SA" lang="EN-IN">Purification and characterization of flavokinase from <i>Neurospora crassa</i></span>

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Title Purification and characterization of flavokinase from Neurospora crassa
 
Creator Rajeswari, Sivalenka Raja
Jonnalagadda, Vidya S
Jonnalagadda, Sobhanaditya
 
Description 137-142
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 Mr 35.5 kDa with maximal
activity at alkaline pH and
high temperature (55°C). The Km 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.
 
Date 2012-12-31T19:21:01Z
2012-12-31T19:21:01Z
1999-06
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15439
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.36(3) [June 1999]