Linked Life Data

8344302

Source:http://linkedlifedata.com/resource/pubmed/id/8344302

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-9-3
pubmed:abstractText
In a previous study [Bulté, L. & Wollman, F.-A. (1992) Eur. J. Biochem. 204, 327-336], we identified a novel gamete-specific polypeptide of Chlamydomonas reinhardtii, M alpha. This 66-kDa polypeptide reacts with antibodies to cytochrome f and accumulates in gametes only in conditions that promote destabilisation of the cytochrome b6/f complex. Here, we show that M alpha is not a modification product of cytochrome f, but is part of protein M, a high-molecular-mass L-amino-acid oxidase located in the periplasm. It catalyzes oxidation of all L-amino acids tested, except cysteine. Using phenylalanine as a substrate, saturation of the enzymatic rate is reached at 2 microM. These characteristics suggest that protein M may operate in vivo as an efficient scavanger of ammonium from extracellular amino acids. The enzyme contains non-covalently bound FAD. It exists in two forms with essentially similar enzymatic properties, of 1.2-1.3 MDa and 0.9-1.0 MDa, respectively. The lighter form is an oligomer of M alpha, while the heavier form contains, in addition to M alpha, a second polypeptide of 135 kDa, M beta, in a molar ratio of 3-4 M alpha/M beta. Both polypeptides are glycosylated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
215
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
351-60
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Extensive accumulation of an extracellular L-amino-acid oxidase during gametogenesis of Chlamydomonas reinhardtii.
pubmed:affiliation
Institut Jacques Monod/CNRS, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't