Aspartate Transcarbamylase from Escherichia coli
نویسندگان
چکیده
منابع مشابه
Subunit structure of aspartate transcarbamylase from Escherichia coli.
1. The molecular weights of the catalytic and regulatory polypeptide chains of aspartate transcarbamylase were determined to be 33,500 and 17,000, respectively. The results of three empirical methods are in good agreement with those obtained by sedimentation equilibrium in guanidine-hydrochloride or derived from the intrinsic viscosity and the sedimentation coefficient measured in the same solv...
متن کاملKinetics of aspartate transcarbamylase from Escherichia coli for the reverse direction of reaction.
The reverse reaction of aspartate transcarbamylase in which phosphate or arsenate is first coupled to carbamyl aspartate, followed by elimination of aspartate, has been studied under conditions in which one product, aspartate, is removed. Aspartate is converted to oxalacetate by glutamate-oxalacetate transaminase, and the resulting oxalacetate is converted to malate by the NADH, NAD+ oxidoreduc...
متن کاملAspartate Transcarbamylase from Leishmania donovani
Leishmania donovani is a protozoal pathogen that belongs to the kinetoplastida order. Unlike in other eucaryotic systems, the first three enzymes of the de novo pyrimidine biosynthetic pathway are not components of a multifunctional protein system. The three enzyme activities in the crude extract were separated on a Sephacryl S-200 column. Aspartate carbamoyltransferase (EC 2.1.3.2) has been pu...
متن کاملThe purification of aspartate transcarbamylase of Escherichia coli and separation of its protein subunits.
Aspartate transcarbamylase, a regulatory enzyme from Escherichia coti, has been prepared by a procedure which yields approximately 5 g of highly purified enzyme from 700 g of wet packed bacterial cells. Purified aspartate transcarbamylase was dissociated by treatment with p-hydroxymercuribenzoate to yield two kinds of protein subunits which were separated by column chromatography. The separated...
متن کاملAspartate transcarbamylase from Escherichia coli. The use of pyridoxal 5'-phosphate as a probe in the active site.
Spectrophotometric titration studies at pH 8.0 have revealed that pyridoxal 5’-phosphate binds as a Schiff base to the catalytic subunit of Escherichia coli aspartate transcarbamylase with a stoichiometry of 3 pyridoxal phosphates per trimer and a dissociation constant of 0.9 pM. The ultraviolet absorption of the Schiff base near 430 nm is lost upon addition of the inhibitor N-(phosphonacetyl)-...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1968
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)93639-2