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PMID: 3548707 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli.

The Biochemical journal ·Vol. 240 ·No. 1 ·1986-11-15 ·Pages 273-6

Hart GJ, Abell C, Battersby AR

Abstract

Hydroxymethylbilane synthase (porphobilinogen deaminase) was purified to apparent homogeneity from Escherichia coli. The enzyme is a monomer of Mr approx. 40,000. The Km for porphobilinogen and relative Vmax. values have been obtained at various pH values over the range 6.2-8.8, enabling pK values for ionizable groups important for activity to be determined. The N-terminal amino acid sequence is presented.

MeSH Terms
Amino Acid Sequence Ammonia-Lyases/isolation & purification Electrophoresis, Polyacrylamide Gel Escherichia coli/enzymology Hydrogen-Ion Concentration Hydroxymethylbilane Synthase/isolation & purification Kinetics Molecular Weight
Chemicals
Hydroxymethylbilane Synthase Ammonia-Lyases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hart G J
Abell C
Battersby A R
References (11)
11 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj2400273
Published
1986-11-15
Pages
273-6
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1147405
Subset
IM
External Links
PubMed source DOI: 10.1042/bj2400273 PMC Full Text View journal details
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