Values CatLog read from this paper

Crystal structure of DmdD, a crotonase superfamily enzyme that catalyzes the hydration and hydrolysis of methylthioacryloyl-CoA

PMID 23704947doi:10.1371/journal.pone.0063870Open 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 7 records (13 values) from this paper: DmdD from Ruegeria pomeroyi.

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. CatLog calculated the 6 kcat/Km values marked “calc.” from kcat and Km; no printed kcat/Km was read for those records.

EC 4.2.1.155

Records read from this paper
EnzymeOrganismSubstratekcat (s⁻¹)Km (mM)kcat/Km (mM⁻¹ s⁻¹)ConditionsOpen record
DmdDRuegeria pomeroyi3-hydroxybutyryl-CoA13.20.119111 calc.pH 7.4Open record: DmdD, 3-hydroxybutyryl-CoA
DmdDRuegeria pomeroyi3-methylmercaptopropionate-CoA0.90.06913 calc.pH 7.4Open record: DmdD, 3-methylmercaptopropionate-CoA
DmdDRuegeria pomeroyiCrotonyl-CoA420.0192.2 × 10³ calc.pH 7.4Open record: DmdD, Crotonyl-CoA
DmdDRuegeria pomeroyimethylthioacryloyl-CoACoA ester hydrolysis (CoA release measured by HPLC); Table 2440.00825.4 × 10³ calc.pH 7.4Open record: DmdD, methylthioacryloyl-CoA
DmdDRuegeria pomeroyimethylthioacryloyl-CoATable 2470.00945.0 × 10³ calc.pH 7.4Open record: DmdD, methylthioacryloyl-CoA
DmdDRuegeria pomeroyimethylthioacryloyl-CoAin the text——5 × 10³pH 7.4Open record: DmdD, methylthioacryloyl-CoA
DmdDvariant E141ARuegeria pomeroyimethylthioacryloyl-CoA0.00360.06330.057 calc.pH 7.4Open record: DmdD variant E141A, methylthioacryloyl-CoA