Abstract:
:The effect of 7-chloro-4-nitrobenzofurazan on yeast 3-phosphoglycerate kinase causes a modification of one tyrosyl residue concomitantly with a total loss of activity of the enzyme. The modification is not accompanied by any significant conformational change. A total protection against inactivation is observed with the substrates : furthermore, AMP, tripolyphosphate and pyrophosphate afford an effective protection. At pH 9, a shift in the absorbance spectrum of the tyrosine O-nitrobenzofurazan derivative of 3-phosphoglycerate kinase is observed. It can be related to the transfer of the reagent from tyrosine to lysine. The N-nitrobenzofurazan derivative is also completely inactive. It is concluded that a lysine residue is located close to the essential tyrosyl residue.
journal_name
Biochimiejournal_title
Biochimieauthors
Roustan C,Fattoum A,Pradel LAdoi
10.1016/s0300-9084(79)80164-9subject
Has Abstractpub_date
1979-01-01 00:00:00pages
663-9issue
5-6eissn
0300-9084issn
1638-6183pii
S0300-9084(79)80164-9journal_volume
61pub_type
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