Linked Life Data

1252412

Source:http://linkedlifedata.com/resource/pubmed/id/1252412

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1976-6-2
pubmed:abstractText
Protocatechuate 3,4-dioxygenase (PCD) from p-hydroxybenzoate-induced cells of Acinetobacter calcoaceticus was purified by heat and protamine sulfate treatment, ammonium sulfate fractionation, DEAE-cellulose, and Sephadex G-200 column chromatography. The enzyme appears to be homogeneous by ultracentrifugation and acrylamide gel electrophoresis. This is the first report of PCD purified from Acinetobacter. For comparison, crystalline Pseudomonas PCD was also obtained. The enzymes from Acinetobacter and Pseudomonas are quite similar in their molecular weight, molecular size, and iron content. The specific enzyme activity of PCD from Acinetobacter is about one-third of that from Pseudomonas, despite their similar iron content. Visible and circular dichroism spectra indicate some conformational differences between these two enzymes. Protocatechualdehyde, a competitive deadend inhibitor, binds Pseudomonas PCD more effectively than Acinetobacter PCD. p-Hydroxymercuribenzoate, specific for free-SH groups, inhibits only Acinetobacter PCD and shows no effect on Pseudomonas PCD. Amino acid analyses reveal very low proline and methionine content with higher lysine, glutamic acid, and isoleucine compositions for Acinetobacter PCD. Other properties, including active center conformation, were studied and discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
582-8
pubmed:dateRevised
2005-11-17
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Protocatechuate 3, 4-dioxygenase from Acinetobacter calcoaceticus.
pubmed:publicationType
Journal Article