Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.1.6.1 (
sulfatase
)
3,205
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The participation of tyramine oxidase in the regulation of
arylsulfatase
synthesis in Klebsiella aerogenes was studied. Arylsulfatase was synthesized when this organism was grown with methionine or taurine as the sulfur source (nonrepressing conditions) and was repressed by inorganic sulfate or cysteine; this repression was relieved by tyramine and related compounds (derepressing conditions). Under nonrepressing conditions,
arylsulfatase
synthesis was not regulated by tyramine oxidase synthesis. However, derepression of
arylsulfatase
and induction of tyramine oxidase synthesis by tyramine were both antagonized by glucose and other carbohydrate compounds. The derepressed synthesis of
arylsulfatase
, like that of tyramine oxidase, was released from catabolite repression by use of tyramine as the sole source of nitrogen. A mutant strain that exhibits constitutive synthesis of
glutamine synthetase
and high levels of histidase when grown in glucose-ammonium medium was subject to the catabolite repression of both tyramine oxidase and
arylsulfatase
syntheses. Mutants in which repression of
arylsulfatase
could not be relieved by tyramine could not utilize tyramine as the sole source of nitrogen and were defective in the gene for tyramine oxidase.
...
PMID:Tyramine oxidase and regulation of arylsulfatase synthesis in Klebsiella aerogenes. 83 Jun 48
The cellular localization of the soluble and membrane-bound forms of the enzyme,
arylsulfatase
(ArS), in rat brain was investigated by measuring their activities in rat striatum after unilateral lesioning with the neurotoxin, kainic acid. Membrane-bound ArS (C form of ArS) activity was found to increase after lesioning and the increase paralleled that of the astroglial marker enzyme,
glutamine synthetase
. Total soluble ArS (A and B forms of ArS) was shown to decrease on day 2 after the kainic acid injection but rapidly increase thereafter. When the two soluble forms of
arylsulfatase
were measured separately, the activity associated with the A form was found to initially decrease followed by a rapid increase in activity, whereas the activity of the B form of the enzyme increased over the entire duration of the experiment. These data suggest that the ArS-C and B form of
arylsulfatase
predominate in proliferating astroglial cells, whereas the A form of
arylsulfatase
is present both in neuronal cell bodies and astroglia associated with the rat striatum.
...
PMID:Cellular localization of soluble and membrane-bound forms of arylsulfatase in rat brain. 289 Apr 6
