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Information on EC 2.5.1.61 - hydroxymethylbilane synthase and Organism(s) Rattus norvegicus and UniProt Accession P19356
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2.5.1.61 hydroxymethylbilane synthaseIUBMB 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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Word Map
- 2.5.1.61
- porphyria
-
intermittent
- heme
- aip
- erythrocyte
-
delta-aminolevulinic
-
5-aminolevulinic
- gapdh
-
erythroid
-
genorm
- urinary
- dehydratase
- protoporphyrin
-
ferrochelatase
-
normfinder
-
housekeeping
- tetrapyrrole
-
bestkeeper
- coproporphyrinogen
-
neurovisceral
-
ywhaz
- protoporphyrinogen
- pyrrole
- variegate
-
photodynamic
-
erythroid-specific
-
half-normal
-
porphyrinogenic
- coproporphyria
- hematin
-
proto
- tarda
- pharmacology
-
beta-2-microglobulin
- hyponatremia
- diagnostics
-
gata-1
- medicine
-
rpl13a
-
lightcycler
-
cutanea
- beta-globin
-
non-erythroid
-
reffinder
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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 i synthetase, uroporphyrinogen synthase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
porphobilinogen ammonia-lyase (polymerizing)
-
-
-
-
pre-uroporphyrinogen synthase
-
-
-
-
synthase, uroporphyrinogen I
-
-
-
-
uroporphyrinogen synthase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
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
9036-47-9
-
9074-91-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
4 porphobilinogen
uroporphyrinogen III + 4 NH3
-
in the presence of uroporphyrinogen III cosynthase, EC 4.2.1.75
-
?
additional information
?
-
-
third enzyme in the heme biosynthetic pathway
-
-
?
additional information
?
-
-
third enzyme in the heme biosynthetic pathway
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
third enzyme in the heme biosynthetic pathway
-
-
?
additional information
?
-
-
third enzyme in the heme biosynthetic pathway
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
protoporphyrin IX
-
enzyme activity decreases with increasing concentrations, reaching a 33% inhibition at the vivo concentration of porphyrin, 0.00185 mM, and 0.014 mM porphobilinogen
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
porphobilinogen
wild type enzyme, at 37°C in Tris-HCl buffer (100 mM, pH 8.0, containing 0.15 mg/ml BSA)
0.066
porphobilinogen
mutant enzyme E63A, at 37°C in Tris-HCl buffer (100 mM, pH 8.0, containing 0.15 mg/ml BSA)
0.24
porphobilinogen
mutant enzyme E63A, at 37°C in Tris-HCl buffer (100 mM, pH 8.0, containing 0.15 mg/ml BSA)
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 8.4
-
pH 6.2: 50% of maximal activity, pH 8.4: 30% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
5 multiple enzyme forms from spleen of phenylhydrazine-treated male rats
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HEM3_RAT
361
0
39361
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D44A
specific activity is only about 2% of that of the wild type enzyme
Q200L
mutant lacks the dipyrromethane cofactor and completely loses the catalytic activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
only a little loss of activity is found even after 1 h preincubation at 60°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 50 mM Tris buffer, pH 7.5, 5% glycerol, and 5 mM beta-mercaptoethanol, 1 year, remains stable
4°C, 50 mM Tris buffer, pH 7.5, 5% glycerol, and 5 mM beta-mercaptoethanol, 1 week, without significant change of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Williams, D.C.
Characterization of the multiple forms of hydroxymethylbilane synthase from rat spleen
Biochem. J.
217
675-683
1984
Rattus norvegicus
Farmer, D.J.; Hollebone, B.R.
Comparative inhibition of hepatic hydroxymethylbilane synthase by both hard and soft metal cations
Can. J. Biochem. Cell Biol.
62
49-54
1984
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Mazzetti, M.B.; Tomio, J.M.
Purification and some properties of rat liver uroporphyrinogen I synthase
Anal. Asoc. Quim. Argent.
76
207-215
1988
Chlorella regularis, Escherichia coli, Homo sapiens, Rattus norvegicus, Spinacia oleracea
-
Sharif, A.; Smith, A.G.; Abell, C.
Isolation and characterisation of cDNA clone for chlorophyll synthesis enzyme from Euglena gracilis
Eur. J. Biochem.
184
353-359
1989
Escherichia coli, Euglena gracilis, Homo sapiens, Rattus norvegicus
Juknat, A.A.; Doernemann, D.; Senger, H.
Purification and kinetic studies on a porphobilinogen deaminase from the unicellular green alga Scenedesmus obliquus
Planta
193
123-130
1994
Saccharomyces cerevisiae, Chlorella regularis, Escherichia coli, Euglena gracilis, Homo sapiens, Pisum sativum, Rattus norvegicus, Cereibacter sphaeroides, Tetradesmus obliquus, Spinacia oleracea
-
Cardalda, C.A.; Juknat, A.A.; Princ, F.G.; Batlle, A.
Rat harderian gland porphobilinogen deaminase: characterization studies and regulatory action of protoporphyrin IX
Arch. Biochem. Biophys.
347
69-77
1997
Rattus norvegicus
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