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Literature summary for 3.2.2.22 extracted from

  • Severino, V.; Chambery, A.; Di Maro, A.; Marasco, D.; Ruggiero, A.; Berisio, R.; Giansanti, F.; Ippoliti, R.; Parente, A.
    The role of the glycan moiety on the structure-function relationships of PD-L1, type 1 ribosome-inactivating protein from P. dioica leaves (2010), Mol. Biosyst., 6, 570-579.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of isozymes in Escherichia coli strain BL21(DE3). Synthesis and expression of a PD-L1 synthetic gene in Escherichia coli strain BL21(DE3) Phytolacca dioica

Organism

Organism UniProt Comment Textmining
Phytolacca dioica P84853 several RIP isoforms, e.g. PD-L1/PD-L2 and PD-L3/PD-L4
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the isozymes differ in their N-glycosylation pattern, overview Phytolacca dioica

Purification (Commentary)

Purification (Comment) Organism
recombinant isozymes from Escherichia coli strain BL21(DE3), purification after overexpression affords refolding by glutathione in refolding buffer, followd by ultrafiltration and cation exchange chromatography Phytolacca dioica

Source Tissue

Source Tissue Comment Organism Textmining
leaf
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Phytolacca dioica
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme inhibits protein synthesis in a rabbit reticulocyte. Structure-function relationship, influence of carbohydrate moieties, overview Phytolacca dioica ?
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Subunits

Subunits Comment Organism
More isozyme structure analysis by ESI/Q-TOF mass spectrometric and circular dichroism analysis, structure-function relationship, influence of carbohydrate moieties, overview Phytolacca dioica

Synonyms

Synonyms Comment Organism
PD-L1
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Phytolacca dioica
type 1 ribosome-inactivating protein
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Phytolacca dioica