Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina barkeri MS and Methanococcus vannielii

Morris, Christina; Reeve, John N.

doi:10.1128/jb.170.7.3125-3130.1988

Cited by 27 publications

(13 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ASS cDNA sequence is known for human [Bock et al, 1983;Kobayashi et al, 1990], rat [Surh et al, 1988], cow [Dennis et al, 1989], mouse [Surh et al, 1991], Methanococcus vannielii, Methanosarcina barkeri MS [Morris and Reeve, 1988], Escherichia coli, and Saccharomyses cerevisiae [Van Vliet et al, 1990]. Since there is a remarkable homology in the amino-acid sequences among ASS proteins from the four mammals with a minimum of 94% identity between any two species, a comparison of these sequences provides little insight into critical residues within the sequence.…”

Section: Speculated E¡ect Of the Missense Mutations On Ass Impairmentmentioning

confidence: 97%

Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients

et al. 2003

View full text Add to dashboard Cite

Classical citrullinemia (CTLN1), a rare autosomal recessive disorder, is caused by mutations of the argininosuccinate synthetase (ASS) gene, localized on chromosome 9q34.1. ASS functions as a rate-limiting enzyme in the urea cycle. Previously, we identified 32 mutations in the ASS gene of CTLN1 patients mainly in Japan and the United States, and to date 34 different mutations have been described in 50 families worldwide. In the present study, we report ASS mutations detected in 35 additional CTLN1 families from 11 countries. By analyzing the entire coding sequence and the intron-exon boundaries of the ASS gene using RT-PCR and/or genomic DNA-PCR, we have identified 16 novel mutations (two different 1-bp deletions, a 67-bp insertion, and 13 missense) and have detected 12 known mutations. Altogether, 50 different mutations (seven deletion, three splice site, one duplication, two nonsense, and 37 missense) in 85 CTLN1 families were identified. On the basis of primary sequence comparisons with the crystal structure of E. coli ASS protein, it may be concluded that any of the 37 missense mutations found at 30 different positions led to structural and functional impairments of the human ASS protein. It has been found that three mutations are particularly frequent: IVS6-2A>G in 23 families (Japan: 20 and Korea: three), G390R in 18 families (Turkey: six, U.S.: five, Spain: three, Israel: one, Austria: one, Canada: one, and Bolivia: one), and R304W in 10 families (Japan: nine and Turkey: one). Most mutations of the ASS gene are "private" and are distributed throughout the gene, except for exons 5 and 12-14. It seems that the clinical course of the patients with truncated mutations or the G390R mutation is early-onset/severe. The phenotype of the patients with certain missense mutations (G362V or W179R) is more late-onset/mild. Eight patients with R86H, A118T, R265H, or K310R mutations were adult/late-onset and four of them showed severe symptoms during pregnancy or postpartum. However, it is still difficult to prove the genotype-phenotype correlation, because many patients were compound heterozygotes (with two different mutations), lived in different environments at the time of diagnosis, and/or had several treatment regimes or various knowledge of the disease.

show abstract

Section: Speculated E¡ect Of the Missense Mutations On Ass Impairmentmentioning

confidence: 97%

Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients

et al. 2003

View full text Add to dashboard Cite

show abstract

“…Sequence comparisons of a number of archaebacterial genes for amino acid biosynthetic enzymes have demonstrated homology with the eubacterial and eucaryotic enzymes (3,5,8,26,31). Therefore, it is likely that many of these enzyme systems in the three major lineages were derived from a common ancestor (19).…”

Section: Discussionmentioning

confidence: 99%

Characterization of enzymes of the branched-chain amino acid biosynthetic pathway in Methanococcus spp

Xing

Whitman

1991

J Bacteriol

View full text Add to dashboard Cite

Methanococcus aeolicus, Methanococcus maripaludis, and Methanococcus voltae contain similar levels of four enzymes of branched-chain amino acid biosynthesis: acetohydroxy acid synthase, acetohydroxy acid isomeroreductase, dihydroxy acid dehydratase, and transaminase B. Following growth at low partial pressures of H2-CO2, the levels of these enzymes in extracts of M. voltae are reduced three-to fivefold, which suggests that their synthesis is regulated. The enzymes from M. aeolicus were found to be similar to the eubacterial and eucaryotic enzymes with respect to molecular weights, pH optima, kinetic properties, and sensitivities to 02. The acetohydroxy acid isomeroreductase has a specific requirement for Mg2+, and other divalent cations were inhibitory. It was stimulated threefold by K+ and NH4+ ions and was able to utilize NADH as well as NADPH.The partially purified enzyme was not sensitive to 2. The dihydroxy acid dehydratase is extremely sensitive to 02and it has a half-iffe under 5% 02 of 6 min at 25°C. Divalent cations were required for activity, and Mg2+, Mn2+, Ni2+, Co2+, and Fe2+ were nearly equally effective. In conclusion, the archaebacterial enzymes are functionally homologous to the eubacterial and eucaryotic enzymes, which implies that this pathway is very ancient.The biosynthesis of the branched-chain amino acids (BCAAs), valine, isoleucine, and leucine, occurs by a parallel set of reactions that is similar in the eubacteria and eucaryotes (for reviews see references 37 and 38 Preparation of extracts and partial purification of enzymes. Extracts of the methanococci were prepared by thawing frozen cells in anaerobic lysis buffer containing 25 mM PIPES [potassium piperazine-N,N'-bis(2-ethanesulfonic acid), pH 6.8], 1 mM dithiothreitol, 1 mM cysteine hydrochloride, and pancreatic DNase (1 mg/100 ml of cell suspension) and centrifuging at 39,000 x g for 20 min at 4°C (42). Freezethawing of these cells was sufficient to disrupt the protein cell wall and produce cell-free extracts. For some experiments, unfrozen extracts were prepared by suspending cells in the anaerobic lysis buffer immediately after harvesting. In buffers containing low concentrations of Na+, these cells rapidly lysed. However, the yield of extract was slightly lower than in extracts prepared by freezing. Dialyzed extracts were prepared as described previously (42). Oxygen was removed from the buffers by flushing with N2 gas for at least 60 min, and strictly anaerobic procedures were used for all purification steps. Chromatography procedures were performed in an anaerobic chamber (Coy Laboratory Products, Ann Arbor, Mich.) in a 5°C cold room. Plastic centrifuge tubes were incubated for at least 24 h in the anaerobic chamber before use to remove dissolved oxygen.After centrifugation, saturated ammonium sulfate (pH 7.5) in water was added slowly to 45 ml of extract at 5°C. The final concentration of ammonium sulfate was 50% of saturation. The solution was mixed slowly for 20 min and centrifuged for 30 min at 30,000 x g at 4°C. The super...

show abstract

“…It was suggested by the above observation that both the divergence between BC and CPS and the internal duplication of CPS had occurred before the divergence between prokaryotes and eukaryotes. (14) Methanosarcina barkeri carbamoyl-phosphatesynthetase N-terminal domain [33], (15) rat carbamoyl-phosphate-synthetase C-terminal domain [27], (16) syrian hamster carbamoylphosphate-synthetase C-terminal domain [28], (17) Drosophila rnelanogaster rudimentary gene product C-terminal domain [29], (1 8) yeast carbamoyl-phosphate-synthetase 1 C-terminal domain [30], (19) [32]. (B) Unrooted phylogenetic tree of CCP and lipoyl domains.…”

Section: Methodsmentioning

confidence: 99%

Molecular evolution of biotin‐dependent carboxylases

Toh

Kondo

Tanabe

1993

European Journal of Biochemistry

View full text Add to dashboard Cite

Amino-acid sequences of three functional units from various biotin-dependent carboxylases, biotin carboxylase, biotin-carboxyl-carrier protein and carboxyl transferase, were investigated by computer-assisted sequence comparison to obtain information about the structure, function, and molecular evolution of the enzymes. Biotin-dependent carboxylases, except transcarboxylase and oxaloacetate decarboxylase which lack biotin carboxylase, exert their catalytic activities through the three functional units. The three functional units correspond with functional domains or subunits of the enzymes, and the genetic information for the units is encoded in different ways from enzyme to enzyme. It is known that biotin carboxylase is homologous to carbamoyl-phosphate synthetase, and that the biotin-carboxyl-carrier protein is homologous to lipoic-acid-binding domain. The evolutionary relationships between the functional units and their homologues were described. A model for the evolutionary history of the enzymes was proposed by molecular phylogenetic analysis, which shows how a wide variety of domain andor subunit structures for the enzymes may have been established. A repeated structure was found in biotin-carboxyl-carrier protein, and the secondary structure of the protein was predicted using the observed sequence similarity with a lipoic-acidbinding domain.The biotin-dependent carboxylases constitute a diverse group of enzymes, which includes acetyl-CoA carboxylase, propionyl-CoA carboxylase, oxaloacetate decarboxylase, pyruvate carboxylase and transcarboxylase. The enzymes are involved in a variety of essential metabolic pathways such as lipogenesis, gluconeogenesis and amino-acid metabolism. In addition, these enzymes have been identified in animals,

show abstract

Conservation of structure in the human gene encoding argininosuccinate synthetase and the argG genes of the archaebacteria Methanosarcina barkeri MS and Methanococcus vannielii

Cited by 27 publications

References 24 publications

Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients

Identification of 16 novel mutations in the argininosuccinate synthetase gene and genotype-phenotype correlation in 38 classical citrullinemia patients

Characterization of enzymes of the branched-chain amino acid biosynthetic pathway in Methanococcus spp

Molecular evolution of biotin‐dependent carboxylases

Contact Info

Product

Resources

About