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dc.contributor.author
Gomez Casati, Diego Fabian
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dc.contributor.author
Sesma, Juliana
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dc.contributor.author
Iglesias, Alberto Alvaro
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dc.date.available
2019-10-11T12:14:40Z
dc.date.issued
2000-05
dc.identifier.citation
Gomez Casati, Diego Fabian; Sesma, Juliana; Iglesias, Alberto Alvaro; Structural and kinetic characterization of NADP-dependent, non- phosphorylating glyceraldehyde-3-phosphate dehydrogenase from celery leaves; Elsevier Ireland; Plant Science; 154; 2; 5-2000; 107-115
dc.identifier.issn
0168-9452
dc.identifier.uri
http://hdl.handle.net/11336/85665
dc.description.abstract
NADP-dependent, non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.9) from celery leaves was purified over 1200-fold to a specific activity of 35 units/mg protein, and its kinetic, regulatory and structural properties were characterized. The purified enzyme exhibited a homotetrameric structure with a subunit molecular mass of 54 kDa. A high specificity of the enzyme for the substrates NADP+ (K(m) = 7 μM) and D- glyceraldehyde-3-phosphate (K(m) = 127 μM) was observed. Maximal activity was determined at pH 8.5. The purified enzyme was highly unstable, requiring the addition of NADP+ or conditions of high ionic strength in the medium. A hysteretic behavior, with a lag phase of minutes, was observed during activity measurement of the enzyme preincubated in the absence of substrates. The lag was inversely proportional to the protein concentration during preincubation. The hysteretic parameters were affected by the substrates, KCl and mannitol among other compounds. Distinctively, incubation with NADP+ produced a near twofold activation of the enzyme. Results suggest that in alditol producing plants the enzyme plays a key role in the synthesis and partitioning of photoassimilates.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Ireland
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
ALDITOLS BIOSYNTHESIS
dc.subject
CARBON PARTITIONING
dc.subject
CELERY LEAVES
dc.subject
GLYCERALDEHYDE- 3-PHOSPHATE DEHYDROGENASE
dc.subject
NON-PHOSPHORYLATING
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Structural and kinetic characterization of NADP-dependent, non- phosphorylating glyceraldehyde-3-phosphate dehydrogenase from celery leaves
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-10T19:33:47Z
dc.journal.volume
154
dc.journal.number
2
dc.journal.pagination
107-115
dc.journal.pais
Irlanda
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dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Gomez Casati, Diego Fabian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
dc.description.fil
Fil: Sesma, Juliana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
dc.description.fil
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
dc.journal.title
Plant Science
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.ncbi.nlm.nih.gov/pubmed/?term=Structural+and+kinetic+characterization+of+NADP-dependent%2C+non-phosphorylating+glycerladehyde-3-phosphate+dehydrogenase+from+celery+leaves
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/S0168-9452(99)00241-1
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