Characterization of porphobilinogen synthase from an aerobic photosynthetic bacterium, erythrobacter sp. strain OCh 114

Yuzo Shioi, Michio Doi

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Porphobilinogen synthase (formerly 5-aminolevulinic acid dehydratase, EC 4.2.1.24) was purified 7,405-fold from an aerobic photosynthetic bacterium, Erythrobacter sp. strain OCh 114. The molecular weight of the enzyme was determined to be 260,000 by Sephadex G-200 gel filtration. The enzyme had a single pH optimum at 8.0 and showed no requirement for metal ion and thiol compound for its maximum activity. The Km value for 5-aminolevulinic acid was 0.29 mM. 4,5-Dioxovaleric acid and levulinic acid were found to be competitive inhibitors of the enzyme, with Ki values of 0.65 and 0.80 mM, respectively. The enzyme was extremely labile in acidic pH and almost completely lost its activity within 1 h at pH 6.0 and 30°C. This Erythrobacter enzyme seems to be similar to the enzyme from the anaerobic photosynthetic bacterium Rhodobacter capsulatus in its molecular and catalytic properties.

Original languageEnglish
Pages (from-to)843-848
Number of pages6
JournalPlant and Cell Physiology
Volume29
Issue number5
Publication statusPublished - Jul 1 1988

Fingerprint

Sphingomonadaceae
Erythrobacter
porphobilinogen synthase
Porphobilinogen Synthase
Aerobic Bacteria
photosynthetic bacteria
Enzymes
enzymes
aminolevulinic acid
Rhodobacter capsulatus
levulinic acid
Aminolevulinic Acid
Anaerobic Bacteria
enzyme inhibitors
Enzyme Inhibitors
thiols
metal ions
Sulfhydryl Compounds
Gel Chromatography
Molecular Weight

All Science Journal Classification (ASJC) codes

  • Physiology
  • Plant Science
  • Cell Biology

Cite this

Characterization of porphobilinogen synthase from an aerobic photosynthetic bacterium, erythrobacter sp. strain OCh 114. / Shioi, Yuzo; Doi, Michio.

In: Plant and Cell Physiology, Vol. 29, No. 5, 01.07.1988, p. 843-848.

Research output: Contribution to journalArticle

@article{b1b998d2084a494ab8967f4649936238,
title = "Characterization of porphobilinogen synthase from an aerobic photosynthetic bacterium, erythrobacter sp. strain OCh 114",
abstract = "Porphobilinogen synthase (formerly 5-aminolevulinic acid dehydratase, EC 4.2.1.24) was purified 7,405-fold from an aerobic photosynthetic bacterium, Erythrobacter sp. strain OCh 114. The molecular weight of the enzyme was determined to be 260,000 by Sephadex G-200 gel filtration. The enzyme had a single pH optimum at 8.0 and showed no requirement for metal ion and thiol compound for its maximum activity. The Km value for 5-aminolevulinic acid was 0.29 mM. 4,5-Dioxovaleric acid and levulinic acid were found to be competitive inhibitors of the enzyme, with Ki values of 0.65 and 0.80 mM, respectively. The enzyme was extremely labile in acidic pH and almost completely lost its activity within 1 h at pH 6.0 and 30°C. This Erythrobacter enzyme seems to be similar to the enzyme from the anaerobic photosynthetic bacterium Rhodobacter capsulatus in its molecular and catalytic properties.",
author = "Yuzo Shioi and Michio Doi",
year = "1988",
month = "7",
day = "1",
language = "English",
volume = "29",
pages = "843--848",
journal = "Plant and Cell Physiology",
issn = "0032-0781",
publisher = "Oxford University Press",
number = "5",

}

TY - JOUR

T1 - Characterization of porphobilinogen synthase from an aerobic photosynthetic bacterium, erythrobacter sp. strain OCh 114

AU - Shioi, Yuzo

AU - Doi, Michio

PY - 1988/7/1

Y1 - 1988/7/1

N2 - Porphobilinogen synthase (formerly 5-aminolevulinic acid dehydratase, EC 4.2.1.24) was purified 7,405-fold from an aerobic photosynthetic bacterium, Erythrobacter sp. strain OCh 114. The molecular weight of the enzyme was determined to be 260,000 by Sephadex G-200 gel filtration. The enzyme had a single pH optimum at 8.0 and showed no requirement for metal ion and thiol compound for its maximum activity. The Km value for 5-aminolevulinic acid was 0.29 mM. 4,5-Dioxovaleric acid and levulinic acid were found to be competitive inhibitors of the enzyme, with Ki values of 0.65 and 0.80 mM, respectively. The enzyme was extremely labile in acidic pH and almost completely lost its activity within 1 h at pH 6.0 and 30°C. This Erythrobacter enzyme seems to be similar to the enzyme from the anaerobic photosynthetic bacterium Rhodobacter capsulatus in its molecular and catalytic properties.

AB - Porphobilinogen synthase (formerly 5-aminolevulinic acid dehydratase, EC 4.2.1.24) was purified 7,405-fold from an aerobic photosynthetic bacterium, Erythrobacter sp. strain OCh 114. The molecular weight of the enzyme was determined to be 260,000 by Sephadex G-200 gel filtration. The enzyme had a single pH optimum at 8.0 and showed no requirement for metal ion and thiol compound for its maximum activity. The Km value for 5-aminolevulinic acid was 0.29 mM. 4,5-Dioxovaleric acid and levulinic acid were found to be competitive inhibitors of the enzyme, with Ki values of 0.65 and 0.80 mM, respectively. The enzyme was extremely labile in acidic pH and almost completely lost its activity within 1 h at pH 6.0 and 30°C. This Erythrobacter enzyme seems to be similar to the enzyme from the anaerobic photosynthetic bacterium Rhodobacter capsulatus in its molecular and catalytic properties.

UR - http://www.scopus.com/inward/record.url?scp=0004360973&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0004360973&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:0004360973

VL - 29

SP - 843

EP - 848

JO - Plant and Cell Physiology

JF - Plant and Cell Physiology

SN - 0032-0781

IS - 5

ER -