6.3.4.16	A1378T	the carbamoyl-phosphate synthetase deficiency-causing mutation greatly decreases enzyme activity	727610	
6.3.4.16	A438P	inactive	727610	
6.3.4.16	Al38P	the carbamoyl-phosphate synthetase deficiency-causing mutation greatly decreases enzyme activity	727610	
6.3.4.16	C1327A	the mutant shows reduced activity compared to the wild-type enzyme, the mutation significantly alters activity at the domain C ATP site, binding of N-acetylglutamate is affected, overview	693247	
6.3.4.16	C1337A	the mutant shows reduced activity compared to the wild-type enzyme, the mutation significantly alters activity at the domain C ATP site, binding of N-acetylglutamate is affected, overview	693247	
6.3.4.16	D265A	no carbamoyl phosphate synthesis	-, 652334	
6.3.4.16	D265E	about 10% of the specific acitivity of the wild-type enzyme	652334	
6.3.4.16	D265N	about 10% of the specific acitivity of the wild-type enzyme	-, 652334	
6.3.4.16	D810A	no carbamoyl phosphate synthesis	652334	
6.3.4.16	D810E	no carbamoyl phosphate synthesis	652334	
6.3.4.16	D810N	no carbamoyl phosphate synthesis	652334	
6.3.4.16	E261Q	no synthesis of carbonyl phosphate in presence of L-glutamine	652418	
6.3.4.16	G1376S	the mutation has no detectable effect on activity	727610	
6.3.4.16	H262N	no carbamoyl phosphate synthesis	-, 652334	
6.3.4.16	H807N	about 30% of the specific acitivity of the wild-type enzyme	652334	
6.3.4.16	I316G	about 10% of the specific acitivity of the wild-type enzyme	652334	
6.3.4.16	I316H	no carbamoyl phosphate synthesis	652334	
6.3.4.16	I316S	about 30% of the specific acitivity of the wild-type enzyme	652334	
6.3.4.16	K258L	synthesis of carbonyl phosphate in presence of L-glutamine	652418	
6.3.4.16	L1381S	the mutation is clearly disease-causing (carbamoyl-phosphate synthetase deficiency), since it induces strong enzyme instability	727610	
6.3.4.16	L229G	about 30% of the specific acitivity of the wild-type enzyme	-, 652334	
6.3.4.16	L390R	the mutation is clearly disease-causing (carbamoyl-phosphate synthetase deficiency), since it induces strong enzyme instability	727610	
6.3.4.16	additional information	connstruction of a domain A deleted mutant hCPS_DELTAA and functional characterization, the mutant shows slightly inccreased catalytic efficiency in absence of N-acetylglutamate and a 4fold increased Km for N-acetylglutamate compared to the wild-type enzyme	693489	
6.3.4.16	additional information	construction of deletion mutant lacking the last 13 residues of the carboxyl end, 70% decrease of the enzyme activity in comparison of the full-length protein	651213	
6.3.4.16	additional information	metabolic profiles of CPSI heterozygous mutants, mutations are splice site mutation c.4101 + 2T - C and c.3558 + 1G - C, overview	703281	
6.3.4.16	additional information	overexpression of SIRT5 in mice leads to increased deacetylation and activation of CPS1 protein in liver of transgenic mice compared to wild-type mice. Urea production is upregulated in hepatocytes of SIRT5 transgenic mice	-, 702101	
6.3.4.16	N1437D	site-directed mutagenesis, the mutant enzymes shows reduced activation by N-acetyl-L-glutamate compared to the wild-type enzyme	702142	
6.3.4.16	N1440D	site-directed mutagenesis, the mutant enzymes shows reduced activation by N-acetyl-L-glutamate compared to the wild-type enzyme	702142	
6.3.4.16	N355D	the carbamoyl-phosphate synthetase deficiency-causing mutation greatly decreases enzyme activity	727610	
6.3.4.16	R1262X	a premature stop codon mutation naturally occuring in carbamoyl phosphate synthetase 1 deficiency, CPS1D	702953	
6.3.4.16	R803G	naturally occuring missense mutation involved in carbamoyl phosphate synthetase 1 deficiency, CPS1D	702953	
6.3.4.16	S228A	about 30% of the specific acitivity of the wild-type enzyme	-, 652334	
6.3.4.16	T1391V	site-directed mutagenesis, the mutant enzymes shows reduced activation by N-acetyl-L-glutamate compared to the wild-type enzyme	702142	
6.3.4.16	T1394A	site-directed mutagenesis, the mutant enzymes shows reduced activation by N-acetyl-L-glutamate compared to the wild-type enzyme	702142	
6.3.4.16	T1405N	significant change in CPSI enzymatic function	675859	
6.3.4.16	T1406D	naturally occurring single nucleotide polymorphism, phenotype, overview	693489	
6.3.4.16	T1443A	the carbamoyl-phosphate synthetase deficiency-causing mutation greatly decreases enzyme activity	727610	
6.3.4.16	T344A	the mutation has no detectable effect on activity	727610	
6.3.4.16	T544M	the carbamoyl-phosphate synthetase deficiency-causing mutation greatly decreases enzyme activity	727610	
6.3.4.16	W1410K	site-directed mutagenesis, the mutant binds N-acetyl-L-beta-phenylglutamate at the N-acetyl-L-glutamate binding site	702142	
6.3.4.16	W1410K	site-directed mutagenesis, the mutant enzymes shows reduced activation by N-acetyl-L-glutamate compared to the wild-type enzyme	702142	
6.3.4.16	Y389C	the carbamoyl-phosphate synthetase deficiency-causing mutation greatly decreases enzyme activity	727610