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 language | English |
|---|---|
| Pages (from-to) | 843-848 |
| Number of pages | 6 |
| Journal | Plant and Cell Physiology |
| Volume | 29 |
| Issue number | 5 |
| Publication status | Published - Jul 1 1988 |
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All Science Journal Classification (ASJC) codes
- Physiology
- Plant Science
- Cell Biology
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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 journal › Article
}
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.
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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 -