Human erythrocyte phosphoglucomutase: comparison of the kinetic properties of PGM1 and PGM2 isoenzymes.

Abstract:

:Kinetic properties of PGM1 and PGM2 phosphoglucomutase "primary" isoenzymes from human erythrocytes were studied. The two enzyme forms share a "ping-pong" kinetic mechanism and show similar Km for substrate (glucose 1-P) and cofactor (glucose 1,6-P2). Micromolar concentrations of fructose 1,6-P2 and glycerate 2,3-P2 inhibit both PGM1 and PGM2 isoenzymes to a similar extent. The sole PGM2 form is affected by ribose monophosphates (ribose 1-P and ribose 5-P) that act as mutase inhibitors vs. glucose 1,6-P2 and as apparent activators vs. glucose 1-P. The interaction between PGM2 isoenzyme and ribose monophosphates is discussed in the light of the ability of this form to also display phosphoribomutase activity.

journal_name

Biochimie

journal_title

Biochimie

authors

Ninfali P,Accorsi A,Palma F,Fazi A,Piatti E,Chiarantini L,Fornaini G

doi

10.1016/0300-9084(84)90115-9

subject

Has Abstract

pub_date

1984-09-01 00:00:00

pages

617-23

issue

9-10

eissn

0300-9084

issn

1638-6183

pii

0300-9084(84)90115-9

journal_volume

66

pub_type

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