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Information on EC 2.5.1.61 - hydroxymethylbilane synthase and Organism(s) Mus musculus and UniProt Accession P22907

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EC Tree
IUBMB Comments
The enzyme works by stepwise addition of pyrrolylmethyl groups until a hexapyrrole is present at the active centre. The terminal tetrapyrrole is then hydrolysed to yield the product, leaving a cysteine-bound dipyrrole on which assembly continues. In the presence of a second enzyme, EC 4.2.1.75 uroporphyrinogen-III synthase, which is often called cosynthase, the product is cyclized to form uroporphyrinogen-III. If EC 4.2.1.75 is absent, the hydroxymethylbilane cyclizes spontaneously to form uroporphyrinogen I.
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This record set is specific for:
Mus musculus
UNIPROT: P22907
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
porphobilinogen deaminase, hmbs, hydroxymethylbilane synthase, pbg-d, uro-s, pbg deaminase, uroporphyrinogen i synthase, human porphobilinogen deaminase, uroporphyrinogen synthase, uroporphyrinogen i synthetase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hepatic porphobilinogen deaminase
-
porphobilinogen ammonia-lyase (polymerizing)
-
-
-
-
pre-uroporphyrinogen synthase
-
-
-
-
synthase, uroporphyrinogen I
-
-
-
-
uroporphyrinogen I synthetase
-
-
uroporphyrinogen synthase
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
porphobilinogen:(4-[2-carboxyethyl]-3-[carboxymethyl]pyrrol-2-yl)methyltransferase (hydrolysing)
The enzyme works by stepwise addition of pyrrolylmethyl groups until a hexapyrrole is present at the active centre. The terminal tetrapyrrole is then hydrolysed to yield the product, leaving a cysteine-bound dipyrrole on which assembly continues. In the presence of a second enzyme, EC 4.2.1.75 uroporphyrinogen-III synthase, which is often called cosynthase, the product is cyclized to form uroporphyrinogen-III. If EC 4.2.1.75 is absent, the hydroxymethylbilane cyclizes spontaneously to form uroporphyrinogen I.
CAS REGISTRY NUMBER
COMMENTARY hide
9036-47-9
-
9074-91-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
show the reaction diagram
-
-
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
show the reaction diagram
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
uroporphyrinogen III cosynthase is more heat-labile than porphobilinogen deaminase. Heat-treatment of the porphobilinogen deaminase/uroporphyrinogen III cosynthase enzyme system forms only 2-4% of uroporphyrinogen III
?
4 porphobilinogen + H2O
hydroxylmethylbilane + 4 NH3
show the reaction diagram
-
-
uroporphyrinogen I, uroporphyrinogen
?
porphobilinogen
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4 porphobilinogen + H2O
hydroxymethylbilane + 4 NH3
show the reaction diagram
-
-
-
?
porphobilinogen
?
show the reaction diagram
-
-
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037
porphobilinogen
-
60°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
wild type, lethally irradiated acute intermittent porphyria mice, porphyria mice injected with bone marrow cells from wild type C57BL/6-CD45.1 mice or from acute intermittent porphyria mice
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme deficiency results in overproduction of porphyrin precursors in acute intermittent porphyria
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HEM3_MOUSE
361
0
39344
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partial
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
enzyme over-expression in hepatocytes reduces precursor accumulation, liver-directed gene therapy might offer an alternative to liver transplantation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Levin, E.Y.; Coleman, D.L.
The enzymatic conversion of porphobilinogen to uroporphyrinogen catalyzed by extracts of hematopoietic mouse spleen
J. Biol. Chem.
242
4248-4253
1967
Mus musculus, Spinacia oleracea
-
Manually annotated by BRENDA team
Unzu, C.; Sampedro, A.; Mauleon, I.; Vanrell, L.; Dubrot, J.; de Salamanca, R.E.; Gonzalez-Aseguinolaza, G.; Melero, I.; Prieto, J.; Fontanellas, A.
Porphobilinogen deaminase over-expression in hepatocytes, but not in erythrocytes, prevents accumulation of toxic porphyrin precursors in a mouse model of acute intermittent porphyria
J. Hepatol.
52
417-424
2010
Homo sapiens (P08397), Homo sapiens, Mus musculus (P22907), Mus musculus
Manually annotated by BRENDA team