Search claims · PlantClaims

Mechanismauthor interpretationoriginal resultmeasured

Claim · model-written summary

The authors suggest changes in enzyme activity were caused by changes in enzyme-specific polyribosomal mRNA amount.

Taxon: parsleyPetroselinum crispume1
Gene: enzyme-specific polyribosomal mRNAe0
Outcome: changes in enzyme activitye0

Verbatim

e0
“the changes in enzyme activity were caused by corresponding changes in the amount of enzyme-specific polyribosomal mRNA”
✓ located verbatim in the source · abstract, characters 1233–1352

e1
“parsley (Petroselinum hortense Hoffm.)”
✓ located verbatim in the source · abstract, characters 117–155

Title

Messenger RNA-controlled Increase of Phenylalanine Ammonia-Lyase Activity in Parsley

Joachim Schröder; Brigitte Betz; Klaus Hahlbrock PLANT PHYSIOLOGY 1977. doi:10.1104/pp.60.3.440

Other claims from this paper (6)

Observationobservedoriginal resultmeasured

Claim · model-written summary

The specific activity of the enzyme in Pyrus communis decreased during maturation.

Taxon: Pyrus communisPyrus communist0
Organ / stage: maturatione2
Outcome: specific activity of the enzymee2
Direction: decreasede2

Verbatim

e2
“The specific activity of the enzyme decreased during maturation”
✓ located verbatim in the source · abstract, characters 535–598

t0
“the Pear (Pyrus communis)”
✓ located verbatim in the source · title, characters 34–59

Title

Pectic Enzymes and Development of the Pear (Pyrus communis)

C. W. NAGEL; M. E. PATTERSON Journal of Food Science 1967. doi:10.1111/j.1365-2621.1967.tb01316.x

Other claims from this paper (12)

Observationobservedoriginal resultmeasured

Claim · model-written summary

Olive specific enzyme activity increased during ripening.

Taxon: olivesOleae0
Outcome: specific enzyme activitye0
Direction: increasede0
Qualifier: ripening periode0

Verbatim

e0
“The maturity index, β-glucosidase enzyme activity, total protein content and specific enzyme activity of the olives increased during the ripening period”
✓ located verbatim in the source · abstract, characters 529–681

Title

Phenol content and β-glucosidase activity during the ripening period of olive fruits (Erkence cv.) from different locations

E. Susamcı; Ö. Tuncay; H. Bayraktar; et al. Grasas y Aceites 2024. doi:10.3989/gya.0865231.2017

Other claims from this paper (9)

Observation Olive fruit maturity index increased during ripening.
Observation Olive β-glucosidase enzyme activity increased during ripening.
Observation Olive total protein content increased during ripening.
Observation Olive total phenol content decreased during ripening.
Observation Olive oleuropein content decreased during ripening.
Observation Other phenolic compound contents in olives decreased during ripening.
Association Altitude and fruit location on the tree affected ripening.
Association Lower altitude increased olive enzyme activity.
Association The sea-facing tree side increased olive enzyme activity.

Observationobservedoriginal resultmeasured

Claim · model-written summary

Leaves of a chlorophyll-less mutant had high specific enzyme activity.

Taxon: PeaLathyrus oleraceust0
Material: chlorophyll-less mutante0
Outcome: specific enzyme activitye0
Direction: highe0

Verbatim

e0
“the high specific enzyme activity in leaves of a chlorophyll-less mutant”
✓ located verbatim in the source · abstract, characters 416–488

t0
“Pea Leaves”
✓ located verbatim in the source · title, characters 61–71

t1
“Pea Leaves”
✓ located verbatim in the source · title, characters 61–71

Title

Light Dependent Increase of Triosephosphate Dehydrogenase in Pea Leaves

B. J. Ortwerth; O. J. Koeppe PLANT PHYSIOLOGY 1966. doi:10.1104/pp.41.7.1213

Other claims from this paper (5)

Observationobservedoriginal resultpositivemeasured

Claim · model-written summary

The rice enzyme had higher specific activity than the mammalian one.

Taxon: riceOryza sativae0
Outcome: specific activitye0
Direction: highere0
Comparator: the mammalian onee0

Verbatim

e0
“the rice enzyme has a considerably higher specific activity than the mammalian one”
✓ located verbatim in the source · abstract, characters 512–594

Title

Molecular cloning and characterization of a rice dehydroascorbate reductase

Jun'ichi Urano; Tomofumi Nakagawa; Yasushi Maki; et al. FEBS Letters 2000. doi:10.1016/s0014-5793(99)01768-8

Other claims from this paper (7)

Observation A cDNA for rice glutathione-dependent DHAR was described.
Observation Recombinant Dhar1p made in Escherichia coli was functional.
Observation Database analysis suggested Dhar1p homologs occur in various plants.
Observation Rice Dhar1p showed low similarity to rat DHAR.
Intervention effect High temperature elevated DHAR1 mRNA in rice seedlings.
Intervention effect High temperature elevated Dhar1p protein in rice seedlings.
Intervention effect High temperature elevated DHAR activity in rice seedlings.

Observationobservedoriginal resultpositivemeasured

Claim · model-written summary

Recombinant enzyme specific activity was 182 U/mg, near native enzyme at 171 U/mg.

Taxon: RiceOryza sativat0
Gene: rOsTAGG2Pe0
Outcome: specific activitye0
Value: 182 U/mge0
Qualifier: 171 U/mge0
Comparator: native enzymee0

Verbatim

e0
“The specific activity of rOsTAGG2P (182 U/mg) was close to that of the native enzyme (171 U/mg)”
✓ located verbatim in the source · abstract, characters 1049–1144

t0
“Rice”
✓ located verbatim in the source · title, characters 18–22

Title

Identification of Rice β-Glucosidase with High Hydrolytic Activity towards Salicylic Acid β-D-Glucoside

Nami HIMENO; Wataru SABURI; Shinji WAKUTA; et al. Bioscience Biotechnology and Biochemistry 2013. doi:10.1271/bbb.120889

Other claims from this paper (7)

Observation Recombinant OsTAGG2 yield was 2.1 mg per litre of culture medium.
Observation E. coli recombinant OsTAGG2 had about threefold lower specific activity than native enzyme.
Observation Recombinant OsTAGG2 optimum pH was 3.4.
Observation Recombinant OsTAGG2 optimum temperature was 60 °C.
Observation Enzyme activity persisted after treatments across pH 3.4–9.8.
Observation Enzyme activity persisted after heat treatment below 55 °C.
Observation Native and recombinant OsTAGG2 showed 4.5–4.7-fold higher activity on salicylic acid glucoside than TAG.

Associationobservedoriginal resultmeasured

Claim · model-written summary

Different growth conditions produced differences in leaf enzyme specific activity.

Taxon: Nicotiana tabacumNicotiana tabacumt0
Outcome: specific activity of purified enzymee0
Setting: growth conditionse0

Not reportedDirection

Verbatim

e0
“differences in the growth conditions of plants resulted in differences in specific activity of purified enzyme from their leaves.”
✓ located verbatim in the source · abstract, characters 480–609

t0
“Nicotiana tabacum”
✓ located verbatim in the source · title, characters 68–85

Title

Ribulose 1,5-bisphosphate carboxylase activity in haploid plants of Nicotiana tabacum

S. Bhaskaran; P. J. Burdick; R. H. Smith Journal of Heredity 1987. doi:10.1093/oxfordjournals.jhered.a110400

Other claims from this paper (3)

Observationobservedoriginal resultmeasured

Claim · model-written summary

The enzyme was monomeric with specific activity 2.57 U/mg.

Gene: enzymee0
Outcome: specific activitye0
Value: 2.57 U/mge0

Not reportedTaxon

Verbatim

e0
“The enzyme was a monomeric protein with specific activity of 2.57 U/mg”
✓ located verbatim in the source · abstract, characters 407–477

Title

Purification and Partial Characterization of β-Glucosidase from Fresh Leaves of Tea Plants(Camellia sinensis(L.)O.Kuntze)

Chang Li 生物化学与生物物理学报(英文版) 2005

Other claims from this paper (11)

Observation Tea leaf β-glucosidase was purified 117-fold with 1.26% yield.
Observation SDS-PAGE estimated enzyme molecular mass at about 41 kDa.
Observation FPLC gel filtration estimated enzyme molecular mass at 34 kDa.
Observation Enzyme activity was optimal at 50℃.
Observation The enzyme was stable below 40℃.
Observation The enzyme was active between pH 4.0 and pH 7.0.
Observation The enzyme had optimum activity at pH 5.5.
Observation The enzyme was fairly stable from pH 4.5 to pH 8.0.
Observation The enzyme showed maximum activity toward pNPG.
Observation The enzyme showed low activity toward pNP-Galacto.
Observation The enzyme had no activity toward pNP-Xylo.

Observationobservedoriginal resultpositivemeasured

Claim · model-written summary

Light enhancement of G6PD activity is specific to green callus enzyme.

Taxon: tobaccoNicotiana tabacumt0
Gene: G6PDe0
Outcome: Enhancement of G6PD activity by lighte0
Qualifier: specific for the green callus enzymee0

Verbatim

e0
“Enhancement of G6PD activity by light is specific for the green callus enzyme”
✓ located verbatim in the source · abstract, characters 1261–1338

t0
“Tobacco”
✓ located verbatim in the source · title, characters 100–107

Title

Correlation between Glucose-6-phosphate Dehydrogenase Activity and Photomixotrophic Growth of Green Tobacco Callus Tissue

Furuhashi, Katsuhisa; Usui, Hideo Institutional Repositories DataBase (IRDB) 1986

Other claims from this paper (10)

Intervention effect Light promoted G6PD activity most among the tested enzymes.
Observation G6PD activity increased only under strong light.
Intervention effect DCMU repressed the light-induced G6PD activity increase.
Intervention effect Reillumination rapidly increased G6PD activity after seven days of darkness.
Association Longer dark incubation reduced the increase in G6PD activity.
Mechanism The authors infer a chloroplast light acceptor induces G6PD increase.
Intervention effect Light did not enhance G6PD activity in white tobacco callus XD-6.
Observation White tobacco callus XD-6 grows actively in darkness.
Intervention effect Light does not promote growth of white tobacco callus XD-6.
Mechanism Light-induced G6PD activity is inferred to contribute to photomixotrophic growth.

Observationobservedoriginal resultmeasured

Claim · model-written summary

Tobacco leaf NADP-ME specific activity was 0.95 μmol min -1 mg -1.

Taxon: TobaccoNicotiana tabacumt0
Gene: NADP-Malic Enzymet0
Outcome: specific enzyme activitye0
Value: 0.95 μmol min -1 mg -1e0

Not reportedDirection

Verbatim

e0
“The specific enzyme activity was 0.95 μmol min -1 mg -1 .”
✓ located verbatim in the source · abstract, characters 210–267

t0
“NADP-Malic Enzyme from Tobacco Leaves”
✓ located verbatim in the source · title, characters 27–64

Title

The Enzyme Kinetics of the NADP-Malic Enzyme from Tobacco Leaves

Helena Ryšlavá; Veronika Doubnerová; Karel Muller; et al. Collection of Czechoslovak Chemical Communications 2007. doi:10.1135/cccc20071420

Other claims from this paper (7)

Observation The enzyme pH optimum was 7.1 to 7.4.
Association The apparent Michaelis constant for L-malate depended on ion cofactor.
Association The NADP+ Michaelis constant did not depend on ion cofactor.
Mechanism Mg2+ dependence indicated more than one binding site.
Observation Mn2+ showed positive cooperativity with Hill coefficient 7.5.
Observation Co2+ showed lower cooperativity with Hill coefficient 3.0.
Observation Ni2+ showed lower cooperativity with Hill coefficient 1.3.

“specific activity of the enzyme”

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