Interactions between cholorophyllase, chlorophyll a, plant lipids and Mg2+

Terpstra, Willemke; Lambers, Johannes W.J.

doi:10.1016/0167-4838(83)90006-7

Cited by 37 publications

(17 citation statements)

References 41 publications

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“…These results clearly indicate that a sequential rather than ping-pong mechanism applies to UDPG-SGTase-catalyzed reaction (27). Thus, they confirm our preliminary data obtained with the acetone powder of maize coleoptiles microsomes (29 Additional insight into the reaction mechanism of UDPGSGTase was obtained by a study of the inhibition by the reaction products: UDP and SG.…”

supporting

confidence: 78%

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Regulation by Phospholipids and Kinetic Studies of Plant Membrane-Bound UDP-Glucose Sterol β-d-Glucosyl Transferase

Ullmann¹,

Bouvier-Navé²,

Benveniste³

1987

Plant Physiol.

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Solubilization and partial purification of the microsomal UDP-glucose sterol glucosyl transferase activity from maize coleoptiles by chromatography on DEAE-cellulose resulted in a highly delipidated (>95%) and inactive enzymic preparation. Addition of sterols revealed part of the activity and subsequent addition of phospholipids further increased the activity. Negatively charged phospholipids were shown to be by far the best activators. The purification step also produced the elimination of two interfering microsomal enzymic activities: UDPase and steryl glucoside acyl transferase. The removal of these two enzymic activities was a prerequisite for kinetic studies including product-inhibition studies, since the substrates of these two latter enzymes are the products of UDPG-SGTase activity. The results of the kinetic studies strongly suggest an ordered bi-bi mechanism for the glucosylation of sterols.

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supporting

confidence: 78%

“…Thus, the product-inhibition pattern excludes the possibility of a random bi-bi mechanism for the reaction of sterol glucosylation (27). If UDP is a competitive inhibitor towards UDPG, the sterol glucosylation mechanism is simply ordered, UDPG being the first bound substrate and UDP the last released product.…”

mentioning

confidence: 99%

Regulation by Phospholipids and Kinetic Studies of Plant Membrane-Bound UDP-Glucose Sterol β-d-Glucosyl Transferase

Ullmann¹,

Bouvier-Navé²,

Benveniste³

1987

Plant Physiol.

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“…The level of Chlase activity is affected by internal and external factors (Drazkiewicz, 1994). The increase in Chlase activity has been related with nutritional deficiencies, and physiological status of the plant such as senescent and m aturation, when deorgani zation of the chloroplast helps to put the latent enzyme and the substrates in contact (Terpstra and Lambers, 1983). Therefore a preliminary charac terization of the enzyme, and optimization of the activity assay, are needed before attem pting to study the role of Chlase during ripening of Capsi cum fruits.…”

Section: ; Rüdiger Et Al 1980mentioning

confidence: 99%

“…The method proposed by Terpstra and Lambers (1983) was used with some modifications. One hundred grams of fruits, cleared of seeds, were chopped and extracted with 100 ml of acetone at -2 0 °C by using a homogenizer U ltraturrax T25 (Janke Kunkel IKa-Labortechnik), and left for 15 min at -2 0 °C.…”

Section: Extraction and Partial Purification O F The Enzym Ementioning

confidence: 99%

Properties of Chlorophyllase from Capsicum annuum L. Fruits

Hornero‐Méndez

Mínguez‐Mosquera

2001

Zeitschrift Für Naturforschung C

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Chlorophyll, Chlorophyllase, Capsicum annuumThe in vitro properties of semi-purified chlorophyllase (chlorophyll-chlorophyllido hy drolase, EC 3.1.1.14) from Capsicum annuum fruits have been studied. The enzym e showed an optimum of activity at pH 8.5 and 50 °C. Substrate specificity was studied for chlorophyll (Chi) a, Chi b, pheophytin (Phe) a and Phe b, with K m values of 10.70, 4.04, 2.67 and 6.37 ^im respectively. Substrate inhibition was found for Phe b at concentrations higher than 5 ^m. Chlorophyllase action on Chi a' and Chi b' was also studied but no hydrolysis was observed, suggesting that the mechanism of action depends on the configuration at C-132 in the chloro phyll molecule, with the enzyme acting only on compounds with R132 stereochemistry. The effect of various metals (Mg2+, Hg2+, Cu2+, Zn2+, Co , Fe2+ and Fe3+) was also investigated, and a general inhibitory effect was found, this being more marked for Hg2+ and Fe2+. Func tional groups such as -SH and -S-S-seem ed to participate in the formation o f the enzymesubstrate complex. Chelating ion and the carbonyl group at C3 appeared to be important in substrate recognition by the enzyme. The method for measuring Chlase activity, including HPLC separation of substrate and product, has been optimized.

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“…The method was an adaptation of that used by Terpstra and Lambers (1983). Flavedo tissue (5-10 g) was homogenized with 20 volumes of acetone at 220°C.…”

Section: Clh Activitymentioning

confidence: 99%

An Evaluation of the Basis and Consequences of a Stay-Green Mutation in thenavel negraCitrus Mutant Using Transcriptomic and Proteomic Profiling and Metabolite Analysis

et al. 2008

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A Citrus sinensis spontaneous mutant, navel negra (nan), produces fruit with an abnormal brown-colored flavedo during ripening. Analysis of pigment composition in the wild-type and nan flavedo suggested that typical ripening-related chlorophyll (Chl) degradation, but not carotenoid biosynthesis, was impaired in the mutant, identifying nan as a type C stay-green mutant. nan exhibited normal expression of Chl biosynthetic and catabolic genes and chlorophyllase activity but no accumulation of dephytylated Chl compounds during ripening, suggesting that the mutation is not related to a lesion in any of the principal enzymatic steps in Chl catabolism. Transcript profiling using a citrus microarray indicated that a citrus ortholog of a number of SGR (for STAY-GREEN) genes was expressed at substantially lower levels in nan, both prior to and during ripening. However, the pattern of catabolite accumulation and SGR sequence analysis suggested that the nan mutation is distinct from those in previously described stay-green mutants and is associated with an upstream regulatory step, rather than directly influencing a specific component of Chl catabolism. Transcriptomic and comparative proteomic profiling further indicated that the nan mutation resulted in the suppressed expression of numerous photosynthesis-related genes and in the induction of genes that are associated with oxidative stress. These data, along with metabolite analyses, suggest that nan fruit employ a number of molecular mechanisms to compensate for the elevated Chl levels and associated photooxidative stress.

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Interactions between cholorophyllase, chlorophyll a, plant lipids and Mg2+

Cited by 37 publications

References 41 publications

Regulation by Phospholipids and Kinetic Studies of Plant Membrane-Bound UDP-Glucose Sterol β-d-Glucosyl Transferase

Regulation by Phospholipids and Kinetic Studies of Plant Membrane-Bound UDP-Glucose Sterol β-d-Glucosyl Transferase

Properties of Chlorophyllase from Capsicum annuum L. Fruits

An Evaluation of the Basis and Consequences of a Stay-Green Mutation in thenavel negraCitrus Mutant Using Transcriptomic and Proteomic Profiling and Metabolite Analysis

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