Alpha 2.0
Login Register
» Articles » PMID: 4686921

Rat Liver Aminomalonate Decarboxylase. Identity with Cytoplasmic Serine Hydroxymethylase and Allothreonine Aldolase

Overview
Journal J Biol Chem
Specialty Biochemistry
Date 1973 Feb 25
PMID 4686921
Citations 7
Authors
A G Palekar
S S Tate
A Meister
Affiliations
Soon will be listed here.
Citing Articles

Purification and physicochemical, kinetic and immunological properties of allosteric serine hydroxymethyltransferase from monkey liver.

Ramesh K, Rao N Biochem J. 1980; 187(3):623-36.

PMID: 6821365 PMC: 1162445. DOI: 10.1042/bj1870623.

Metabolic homoeostasis of L-threonine in the normally-fed rat. Importance of liver threonine dehydrogenase activity.

Bird M, Nunn P Biochem J. 1983; 214(3):687-94.

PMID: 6414460 PMC: 1152304. DOI: 10.1042/bj2140687.

Evidence for L-threonine cleavage and allothreonine formation by different enzymes from Clostridium pasteurianum: threonine aldolase and serine hydroxymethyltransferase.

Stocklein W, Schmidt H Biochem J. 1985; 232(2):621-2.

PMID: 3937521 PMC: 1152926. DOI: 10.1042/bj2320621.

L-threonine aldolase is not a genuine enzyme in rat liver.

Yeung Y Biochem J. 1986; 237(1):187-90.

PMID: 3800876 PMC: 1146964. DOI: 10.1042/bj2370187.

A comparison of pyridoxal 5'-phosphate dependent decarboxylase and transaminase enzymes at a molecular level.

Smith D, Thomas N, Gani D Experientia. 1991; 47(11-12):1104-18.

PMID: 1765122 DOI: 10.1007/BF01918374.