Aspartate transcarbamylase from the hyperthermophilic eubacterium Thermotoga maritima: fused catalytic and regulatory polypeptides form an allosteric enzyme.
In the allosteric aspartate transcarbamylase (ATCase) from the hyperthermophilic eubacterium Thermotoga maritima, the catalytic and regulatory functions, which in class B ATCases are carried out by specialized polypeptides, are combined on a single type of polypeptide assembled in trimers. The ATCases from T. maritima and Treponema denticola present intriguing similarities, suggesting horizontal gene transfer.
Chen
P
P
Laboratory for Genetics and Microbiology, Vrije Universiteit Brussel, Brussels, Belgium.
Van Vliet
F
F
Van De Casteele
M
M
Legrain
C
C
Cunin
R
R
Glansdorff
N
N
D000495:Allosteric Site; D000595:Amino Acid Sequence; D001221:Aspartate Carbamoyltransferase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D022761:Gene Transfer, Horizontal; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D020124:Thermotoga maritima / Q000201:enzymology* / Q000235:genetics; D014208:Treponema / Q000201:enzymology / Q000235:genetics
D011994:Recombinant Proteins; D001221:Aspartate Carbamoyltransferase