Values CatLog read from this paper

Co-occurrence of both L-asparaginase subtypes in Arabidopsis: At3g16150 encodes a K+-dependent L-asparaginase

PMID 16705405doi:10.1007/s00425-006-0245-9Open in Browse

The paper itself is not on this site: read it at the publisher. This page lists only the values CatLog read from it.

CatLog read 5 records (15 values) from this paper: K+-independent L-asparaginase At5g08100, K+-dependent L-asparaginase At3g16150 from Arabidopsis thaliana.

Read from the paper by an AI model and checked against the paper by a second, separate AI run; code converted the units. Values are in CatLog's units; each record opens in Browse with the line the paper prints and the checks.

EC 3.5.1.1

Records read from this paper
EnzymeOrganismSubstratekcat (s⁻¹)Km (mM)kcat/Km (mM⁻¹ s⁻¹)ConditionsOpen record
K+-dependent L-asparaginase At3g16150Arabidopsis thalianaL-asparagine63.50.8971.3pH 7.2, 24 °COpen record: K+-dependent L-asparaginase At3g16150, L-asparagine
K+-dependent L-asparaginase At3g16150Arabidopsis thalianaL-aspartic beta-hydroxamate58.31.0854pH 7.3, 37 °COpen record: K+-dependent L-asparaginase At3g16150, L-aspartic beta-hydroxamate
K+-independent L-asparaginase At5g08100Arabidopsis thalianabeta-aspartyl-histidine4.587.690.6pH 7.2, 24 °COpen record: K+-independent L-asparaginase At5g08100, beta-aspartyl-histidine
K+-independent L-asparaginase At5g08100Arabidopsis thalianaL-asparagine3.253.780.86pH 7.2, 24 °COpen record: K+-independent L-asparaginase At5g08100, L-asparagine
K+-independent L-asparaginase At5g08100Arabidopsis thalianaL-aspartic beta-hydroxamate2.4817.30.14pH 7.3, 37 °COpen record: K+-independent L-asparaginase At5g08100, L-aspartic beta-hydroxamate