The crystal structure of adenylosuccinate synthetase from E. coli reveals that the dominant structural element of each monomer of the homodimer is a central beta-sheet of 10 strands. The first nine strands of the sheet are mutually parallel with right-handed crossover connections between the strands. The 10th strand is antiparallel with respect to the first nine strands. In addition, the enzyme has two antiparallel beta-sheets, composed of two strands and three strands each, 11 alpha-helices and two short 310-helices. Further, it has been suggested that the similarities in the GTP-binding domains of the synthetase and the p21ras protein are an example of convergent evolution of two distinct families of GTP-binding proteins.[1]Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana when compared with the known structures from E. coli reveals that the overall fold is very similar to that of the E. coli protein.[2]
Isozymesedit
Humans express two adenylosuccinate synthase isozymes:
Adenylosuccinate+synthase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Referencesedit
^Poland BW, Silva MM, Serra MA, Cho Y, Kim KH, Harris EM, Honzatko RB (December 1993). "Crystal structure of adenylosuccinate synthetase from Escherichia coli. Evidence for convergent evolution of GTP-binding domains". J. Biol. Chem. 268 (34): 25334–42. doi:10.1016/S0021-9258(19)74396-8. PMID 8244965.
^Prade L, Cowan-Jacob SW, Chemla P, Potter S, Ward E, Fonne-Pfister R (February 2000). "Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana". J. Mol. Biol. 296 (2): 569–77. doi:10.1006/jmbi.1999.3473. PMID 10669609.
This article incorporates text from the public domain Pfam and InterPro: IPR001114
adenylosuccinate, synthase, molecular, biology, adenylosuccinate, synthase, adenylosuccinate, synthetase, enzyme, that, plays, important, role, purine, biosynthesis, catalysing, guanosine, triphosphate, dependent, conversion, inosine, monophosphate, aspartic, . In molecular biology adenylosuccinate synthase or adenylosuccinate synthetase EC 6 3 4 4 is an enzyme that plays an important role in purine biosynthesis by catalysing the guanosine triphosphate GTP dependent conversion of inosine monophosphate IMP and aspartic acid to guanosine diphosphate GDP phosphate and N 6 1 2 dicarboxyethyl AMP Adenylosuccinate synthetase has been characterised from various sources ranging from Escherichia coli gene purA to vertebrate tissues In vertebrates two isozymes are present one involved in purine biosynthesis and the other in the purine nucleotide cycle Adenylosuccinate synthaseAdenylosuccinate synthetase dimer HumanIdentifiersEC no 6 3 4 4CAS no 9023 57 8DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteinsAdenylsucc syntstructures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thalianaIdentifiersSymbolAdenylsucc syntPfamPF00709Pfam clanCL0023InterProIPR001114PROSITEPDOC00444SCOP21ade SCOPe SUPFAMAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary Contents 1 Structure 2 Isozymes 3 External links 4 ReferencesStructure editThe crystal structure of adenylosuccinate synthetase from E coli reveals that the dominant structural element of each monomer of the homodimer is a central beta sheet of 10 strands The first nine strands of the sheet are mutually parallel with right handed crossover connections between the strands The 10th strand is antiparallel with respect to the first nine strands In addition the enzyme has two antiparallel beta sheets composed of two strands and three strands each 11 alpha helices and two short 310 helices Further it has been suggested that the similarities in the GTP binding domains of the synthetase and the p21ras protein are an example of convergent evolution of two distinct families of GTP binding proteins 1 Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana when compared with the known structures from E coli reveals that the overall fold is very similar to that of the E coli protein 2 Isozymes editHumans express two adenylosuccinate synthase isozymes adenylosuccinate synthaseIdentifiersSymbolADSSNCBI gene159HGNC292OMIM103060RefSeqNM 001126UniProtP30520Other dataEC number6 3 4 4LocusChr 1 q44Search forStructuresSwiss modelDomainsInterPro adenylosuccinate synthase like 1IdentifiersSymbolADSSL1NCBI gene122622HGNC20093OMIM612498RefSeqNM 152328UniProtQ8N142Other dataEC number6 3 4 4LocusChr 14 q32 33Search forStructuresSwiss modelDomainsInterProExternal links editAdenylosuccinate synthase at the U S National Library of Medicine Medical Subject Headings MeSH References edit Poland BW Silva MM Serra MA Cho Y Kim KH Harris EM Honzatko RB December 1993 Crystal structure of adenylosuccinate synthetase from Escherichia coli Evidence for convergent evolution of GTP binding domains J Biol Chem 268 34 25334 42 doi 10 1016 S0021 9258 19 74396 8 PMID 8244965 Prade L Cowan Jacob SW Chemla P Potter S Ward E Fonne Pfister R February 2000 Structures of adenylosuccinate synthetase from Triticum aestivum and Arabidopsis thaliana J Mol Biol 296 2 569 77 doi 10 1006 jmbi 1999 3473 PMID 10669609 This article incorporates text from the public domain Pfam and InterPro IPR001114 Portal nbsp Biology Retrieved from https en wikipedia org w index php title Adenylosuccinate synthase amp oldid 1172338665, wikipedia, wiki, book, books, library,
