Formaldehyde Binding by 2-Keto-4-hydroxyglutarate Aldolase
Open Access
- 1 August 1974
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 249 (15), 4891-4896
- https://doi.org/10.1016/s0021-9258(19)42405-8
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Variant properties of bovine liver 2-keto-4-hydroxyglutarate aldolase; its β-decarboxylase activity, lack of substrate stereospecificity, and structural requirements for binding substrate analogsBiochimica et Biophysica Acta (BBA) - Enzymology, 1971
- Chromatography of proteins on diethylaminoethyl-cellulose in concentrated ammonium sulfateAnalytical Biochemistry, 1971
- 2-Keto-4-hydroxybutyrate aldolase. Identification as 2-keto-4-hydroxyglutarate aldolase, catalytic properties, and role in the mammalian metabolism of L-homoserineBiochemistry, 1971
- 2-Keto-4-hydroxyglutarate aldolase of bovine liver. Schiff-base formation with 2-keto-4-hydroxyglutarate, pyruvate, and glyoxylateBiochemistry, 1971
- 2-Keto-4-hydroxybutyrate. Synthesis, chemical properties, and as a substrate for lactate dehydrogenase of rabbit muscleBiochemistry, 1969
- 2-Keto-4-hydroxyglutarate Aldolase of Bovine LiverPublished by Elsevier ,1969
- Enzymatic Steps in the Conversion of γ-Hydroxyglutamate to Glyoxylate and AlaninePublished by Elsevier ,1963
- Hydroxyproline MetabolismPublished by Elsevier ,1960
- Hydroxyproline MetabolismPublished by Elsevier ,1960
- A Test for aldehydes using dimethylcyclohexanedioneIndustrial & Engineering Chemistry Analytical Edition, 1931