Biosynthesis of anthraquinones in cell cultures of the Rubiaceae
- Ying Han, R. van der Heijden, R. Verpoorte
- Biology, ChemistryPlant Cell Tissue and Organ Culture
- 1 December 2001
Findings demonstrate that the 2-C-methyl-D-erythritol 4-phosphate pathway, not the mevalonic acid pathway, is involved in the formation of isopentenyl diphosphate, which constitutes ring C of anthraquinones in the Rubiaceae.
Salicylic Acid Enhances Jaceosidin and Syringin Production in Cell Cultures of Saussurea medusa
The results indicate that salicylic acid enhances the production of jaceosidin and syringin which is accompanied by induction of the related phenylpropanoid biosynthetic enzymes.
Oxaloacetate Hydrolase, the C–C Bond Lyase of Oxalate Secreting Fungi*
It is proposed that cellular uptake of this inhibitor could reduce oxalate production because of the mechanism-based, tight binding OAH inhibitor 3,3-difluorooxaloacetate (Ki = 68 nm).
Biosynthesis of anthraquinones in cell cultures of Cinchona 'Robusta' proceeds via the methylerythritol 4-phosphate pathway.
Identification of fungal oxaloacetate hydrolyase within the isocitrate lyase/PEP mutase enzyme superfamily using a sequence marker‐based method
- H. Joosten, Ying Han, W. Niu, J. Vervoort, D. Dunaway-Mariano, P. Schaap
- BiologyProteins: Structure, Function, and Bioinformatics
- 24 July 2007
It is proposed that presence of this serine in family members correlates with presence of OAH activity whereas its absence correlates with absence of OAS, and is tested by carrying out a serine mutagenesis study with the OAH from the fungal oxalic acid producer Botrytis cinerea and the O AH active plant petal death protein as test systems.
Structure and kinetics of phosphonopyruvate hydrolase from Variovorax sp. Pal2: new insight into the divergence of catalysis within the PEP mutase/isocitrate lyase superfamily.
The proposed PPH catalytic mechanism is analogous to that of PEPM but includes activation of a water nucleophile with the loop Thr118 residue and may have favored the open conformation of PPH even when the enzyme was cocrystallized with the oxalate inhibitor.
Cloning of a cDNA encoding 1-deoxy-d-xylulose 5-phosphate synthase from Morinda citrifolia and analysis of its expression in relation to anthraquinone accumulation☆
A missing enzyme in thiamin thiazole biosynthesis: identification of TenI as a thiazole tautomerase.
The function of TenI is identified as a thiazole tautomerase, the structure of the enzyme complexed with its reaction product is described, and the substrates phosphate and histidine 122 as the acid/base residues involved in catalysis are identified.
Effects of elicitation on jaceosidin and hispidulin production in cell suspension cultures of Saussurea medusa
Structure and function of PA4872 from Pseudomonas aeruginosa, a novel class of oxaloacetate decarboxylase from the PEP mutase/isocitrate lyase superfamily.
Genome context of the fourteen sequence family members indicates that the enzyme is used by select group of Gram-negative bacteria to maintain cellular concentrations of bicarbonate and pyruvate; however the decarboxylation activity cannot be attributed to a pathway common to the various bacterial species.