Does aspartate inhibit or stimulate ATCase?

Figure 10.1. ATCase Reaction. Aspartate transcarbamoylase catalyzes the committed step, the condensation of aspartate and carbamoyl phosphate to form N-carbamoylaspartate, in pyrimidine synthesis. John Gerhart and Arthur Pardee found that ATCase is inhibited by CTP, the final product of the ATCase-controlled pathway.

What type of enzyme is aspartate transcarbamoylase?

cytosolic enzyme
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate (CP) to produce N-carbamoyl-L-aspartate (CAA). This reaction is the first committed step of the pyrimidine biosynthetic pathway.

Is aspartate a Transcarbamoylase?

Aspartate carbamoyltransferase (also known as aspartate transcarbamoylase or ATCase) catalyzes the first step in the pyrimidine biosynthetic pathway (EC 2.1. 3.2). In E. coli, the enzyme is a multi-subunit protein complex composed of 12 subunits (300 kDa in total).

What is ATCase substrate?

ATCase is a textbook example of a molecule under allosteric regulation in which the binding of substrate to one active site in a molecule increases the likelihood that the enzyme will bind more substrate, a phenomena called cooperativity.

What is the structure of aspartate transcarbamoylase ( ATCase )?

Aspartate Transcarbamoylase (ATCase) is an allosterically regulated enzyme with unique quaternary structure involving separable catalytic and regulatory subunits. This allosteric regulation affects the kinetics of the enzyme. ATCase consists of two catalytic trimers and three regulatory dimers that are completely separable units.

What is the function of aspartate carbamoyltransferase in E coli?

Aspartate carbamoyltransferase. Aspartate carbamoyltransferase (also known as aspartate transcarbamoylase or ATCase) catalyzes the first step in the pyrimidine biosynthetic pathway (EC 2.1.3.2). In E. coli, the enzyme is a multi-subunit protein complex composed of 12 subunits (300 kDa in total).

Why is aspartate carbamoyltransferase an archetyeric example?

Aspartate carbamoyltransferase. The particular arrangement of catalytic and regulatory subunits in this enzyme affords the complex with strongly allosteric behaviour with respect to its substrates. The enzyme is an archetypal example of allosteric modulation of fine control of metabolic enzyme reactions.

Which is enzyme catalyzes the condensation of carbamoyl phosphate with aspartate?

Aspartate transcarbamoylase (ATCase) catalyzes a key step of pyrimidine biosynthesis, the condensation of carbamoyl phosphate with aspartate to form N -carbamoylaspartate. The Escherichia coli enzyme has been extensively studied.