aspartate carbamoyltransferase
aspartate transcarbamoylase , ATCase (skrót)

Aspartate carbamoyltransferase was a much larger molecule than anything solved previously.

Aspartate carbamoyltransferase is a complex of twelve molecules.

Aspartate carbamoyltransferase has a αβ subunit composition.

Aspartate carbamoyltransferase.

Aspartate carbamoyltransferase performs a step in building the pyrimidine nucleotides (cytosine and thymidine).

CTP also acts as an inhibitor of the enzyme Aspartate carbamoyltransferase, which is used in pyrimidine biosynthesis.

In a subsequent cyclization reaction, the enzyme Aspartate carbamoyltransferase forms N-carbamoyl-aspartate which is converted into dihydroorotic acid by dihydroorotase.

More recently, the E. coli enzyme aspartate carbamoyltransferase (ATCase) has become another good example of allosteric regulation.

Aspartate carbamoyltransferase (ATCase) catalyses the conversion of aspartate and carbamoyl phosphate to carbamoylaspartate, the second step in the de novo biosynthesis of pyrimidine nucleotides.

The three genes that are fused together in the unikonts but not bacteria or bikonts encode enzymes for synthesis of the pyrimidine nucleotides: carbamoyl phosphate synthase, dihydroorotase, aspartate carbamoyltransferase.

Aspartate carbamoyltransferase also ensures that just the right amount of pyrimidine nucleotides is available, as activator and inhibitor molecules attach to aspartate carbamoyltransferase to speed it up and to slow it down.

After obtaining his Ph.D., Stevens accepted a postdoctoral position in 1988 in the lab of Nobel Laureate William N. Lipscomb, Jr. in the chemistry department at Harvard University where he focused on the large allosteric enzyme aspartate carbamoyltransferase.