The enzyme histidinol-phosphatase (EC 3.1.3.15)
catalyzes
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recyc ...
the reaction
:
L-histidinol phosphate + H
2O
L-histidinol + phosphate
This enzyme participates in
histidine metabolism
Histidine (symbol His or H) is an essential amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated –NH3+ form under biological conditions), a carboxylic acid group (which is in the de ...
.
Nomenclature
This enzyme belongs to the family of
hydrolases, to be specific, those acting on phosphoric
monoester
In chemistry, an ester is a compound derived from an oxoacid (organic or inorganic) in which at least one hydroxyl group () is replaced by an alkoxy group (), as in the substitution reaction of a carboxylic acid and an alcohol. Glycerides are fa ...
bonds. The
systematic name is
L-histidinol-phosphate phosphohydrolase. Other names in common use include histidinol phosphate phosphatase,
L-histidinol phosphate phosphatase, histidinolphosphate phosphatase, HPpase, and histidinolphosphatase.
''E. coli''
In ''E. coli'' the enzyme encoded by the gene ''
hisB
The hisB gene, found in the enterobacteria (such as '' E. coli''), in ''Campylobacter jejuni'' and in '' Xylella''/''Xanthomonas'' encodes a protein involved in catalysis of two step in histidine biosynthesis (the sixth and eight step), namely the ...
'' is a fused
imidazoleglycerol-phosphate dehydratase
The enzyme imidazoleglycerol-phosphate dehydratase () catalyzes the chemical reaction
:D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate \rightleftharpoons 3-(imidazol-4-yl)-2-oxopropyl phosphate + H2O
This enzyme belongs to the family of lyases, ...
and histidinol-phosphatase.
References
Further reading
*
EC 3.1.3
Enzymes of known structure
{{3.1-enzyme-stub