RGD Reference Report - Characterization of porphobilinogen deaminase from rat liver. - Rat Genome Database

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Characterization of porphobilinogen deaminase from rat liver.

Authors: Mazzetti, MB  Tomio, JM 
Citation: Mazzetti MB and Tomio JM, Biochim Biophys Acta. 1988 Nov 2;957(1):97-104.
RGD ID: 2301707
Pubmed: PMID:3179323   (View Abstract at PubMed)

Porphobilinogen deaminase (porphobilinogen ammonia-lyase, EC 4.3.1.8) was isolated from rat liver. The final preparation was homogeneous according to polyacrylamide gel electrophoresis and immunodiffusion criteria. Electrophoresis of the native enzyme revealed a single band of activity which was distributed into three bands after incubation with porphobilinogen. When electrophoresed under denaturing condition it displayed a single polypeptide band with a molecular weight of 42,000 confirmed by exclusion chromatography and by sucrose density gradient centrifugation. The enzyme showed a pH optimum of 7.5 both in 0.1 M sodium phosphate and 0.05 M Tris-HCl buffer, when assayed at 37 degrees C. An isoelectric point of 4.9 for the native purified protein was found. Hepatic porphobilinogen deaminase was remarkably heat-stable showing maximum activity at 55-60 degrees C with one break in the Arrhenius plot. The kinetic behaviour of the purified enzyme followed the typical Michaelis-Menten kinetics with values of Km = 17 microM and Vmax = 29.4 units power mg in 0.1 M phosphate buffer at 37 degrees C. The amino acid composition was determined, showing that the enzyme had a low content of sulphur-containing amino acids and a considerable number of acidic residues per mol of polypeptide chain. Reagents known to interact with sulphydryl groups have small effect on rat liver enzyme activity.



Gene-Chemical Interaction Annotations    Click to see Annotation Detail View

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
HMBSHumanp-chloromercuribenzoic acid increases activityISORGD:2801p-chloromercuribenzoic acid increases activity of purified Hmbs proteinRGD 
HmbsRatp-chloromercuribenzoic acid increases activityEXP p-chloromercuribenzoic acid increases activity of purified Hmbs proteinRGD 
HmbsMousep-chloromercuribenzoic acid increases activityISORGD:2801p-chloromercuribenzoic acid increases activity of purified Hmbs proteinRGD 

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
HmbsRatporphyrin-containing compound biosynthetic process  IDA Uroporphyrin IRGD 
HmbsRatporphyrin-containing compound metabolic process  IDA Porphobilinogen RGD 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
HmbsRathydroxymethylbilane synthase activity  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Hmbs  (hydroxymethylbilane synthase)

Genes (Mus musculus)
Hmbs  (hydroxymethylbilane synthase)

Genes (Homo sapiens)
HMBS  (hydroxymethylbilane synthase)


Additional Information