Ferrous ion activates the less active form of human adrenal tyrosine hydroxylase.

Abstract:

:The less active form of human tyrosine hydroxylase has been previously reported but its physiological role is unknown. We partially purified the less active form of tyrosine hydroxylase from human adrenals, and examined differences in the properties of the active and less active forms. We succeeded in activation of the less active form of human tyrosine hydroxylase by addition of 100 ?M Fe(2+). Fe(2+) decreased the K(max) for pteridine cofactor in both the active and less active forms, but increased the V(max) only in the less active form. Fe(2+) changed the V(max) but not the K(m) of the less active form for tyrosine. These results suggest that Fe(2+) may regulate tyrosine hydroxylase activity in vivo as a result of activation of its less active form.

journal_name

Neurochem Int

authors

Ishii A,Kiuchi K,Matsuyama M,Satake T,Nagatsu T

doi

10.1016/0197-0186(90)90123-b

subject

Has Abstract

pub_date

1990-01-01 00:00:00

pages

59-64

issue

1

eissn

0197-0186

issn

1872-9754

pii

0197-0186(90)90123-B

journal_volume

16

pub_type

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