Spatial proximity of a tyrosyl and a lysyl residue in the active site region of yeast 3-phosphoglycerate kinase.

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

Biochimie

journal_title

Biochimie

authors

Roustan C,Fattoum A,Pradel LA

doi

10.1016/s0300-9084(79)80164-9

subject

Has Abstract

pub_date

1979-01-01 00:00:00

pages

663-9

issue

5-6

eissn

0300-9084

issn

1638-6183

pii

S0300-9084(79)80164-9

journal_volume

61

pub_type

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