アデニロコハク酸合成酵素、アデニロコハク酸シンターゼ
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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/06/19 19:00:36」(JST)
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| Adenylosuccinate synthase |
| Identifiers |
| EC number |
6.3.4.4 |
| CAS number |
9023-57-8 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Gene Ontology |
AmiGO / EGO |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
|
| Adenylsucc_synt |
|
structures of adenylosuccinate synthetase from triticum aestivum and arabidopsis thaliana
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| Identifiers |
| Symbol |
Adenylsucc_synt |
| Pfam |
PF00709 |
| Pfam clan |
CL0023 |
| InterPro |
IPR001114 |
| PROSITE |
PDOC00444 |
| SCOP |
1ade |
| SUPERFAMILY |
1ade |
| Available protein structures: |
| Pfam |
structures |
| PDB |
RCSB PDB; PDBe; PDBj |
| PDBsum |
structure summary |
|
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.
Contents
- 1 Structure
- 2 Isozymes
- 3 External links
- 4 References
Structure
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 3/10-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
Humans express two adenylosuccinate synthase isozymes:
| adenylosuccinate synthase |
| Identifiers |
| Symbol |
ADSS |
| Entrez |
159 |
| HUGO |
292 |
| OMIM |
103060 |
| RefSeq |
NM_001126 |
| UniProt |
P30520 |
| Other data |
| EC number |
6.3.4.4 |
| Locus |
Chr. 1 q44 |
|
| adenylosuccinate synthase like 1 |
| Identifiers |
| Symbol |
ADSSL1 |
| Entrez |
122622 |
| HUGO |
20093 |
| OMIM |
612498 |
| RefSeq |
NM_152328 |
| UniProt |
Q8N142 |
| Other data |
| EC number |
6.3.4.4 |
| Locus |
Chr. 14 q32.33 |
|
External links
- Adenylosuccinate synthase at the US National Library of Medicine Medical Subject Headings (MeSH)
References
- ^ 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. 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
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Enzymes: CO CS and CN ligases (EC 6.1-6.3)
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|
| 6.1: Carbon-Oxygen |
- Aminoacyl tRNA synthetase
- Alanine
- Arginine
- Asparagine
- Aspartate
- Cysteine
- D-alanine—poly(phosphoribitol) ligase
- Glutamate
- Glutamine
- Glycine
- Histidine
- Isoleucine
- Leucine
- Lysine
- Methionine
- Phenylalanine
- Proline
- Serine
- Threonine
- Tryptophan
- Tyrosine
- Valine
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|
| 6.2: Carbon-Sulfur |
- Succinyl coenzyme A synthetase
- Acetyl—CoA synthetase
- Long-chain-fatty-acid—CoA ligase
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|
| 6.3: Carbon-Nitrogen |
- Glutamine synthetase
- Ubiquitin ligase
- Cullin
- Von Hippel–Lindau tumor suppressor
- UBE3A
- Mdm2
- Anaphase-promoting complex
- UBR1
- Glutathione synthetase
- CTP synthetase
- Adenylosuccinate synthase
- Argininosuccinate synthase
- Holocarboxylase synthetase
- GMP synthase
- Asparagine synthetase
- Carbamoyl phosphate synthetase
- Glutamate–cysteine ligase
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|
- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Ligases: carbon-carbon ligases (EC 6.4)
|
|
| Biotin dependent carboxylation |
- Pyruvate carboxylase
- Acetyl-CoA carboxylase
- Propionyl-CoA carboxylase
- Methylcrotonyl-CoA carboxylase
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| Other |
|
|
- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Enzymes: Phosphoric ester and nitrogen-metal ligases (EC 6.5-6.6)
|
|
| 6.5: Phosphoric Ester |
|
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| 6.6: Nitrogen-Metal |
- Magnesium chelatase
- Cobalt chelatase
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|
- Biochemistry overview
- Enzymes overview
- By EC number: 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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- Metabolism: amino acid metabolism
- nucleotide enzymes
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| Purine metabolism |
| Anabolism |
| R5P→IMP: |
- Ribose-phosphate diphosphokinase
- Amidophosphoribosyltransferase
- Phosphoribosylglycinamide formyltransferase
- AIR synthetase (FGAM cyclase)
- Phosphoribosylaminoimidazole carboxylase
- Phosphoribosylaminoimidazolesuccinocarboxamide synthase
- IMP synthase
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|
| IMP→AMP: |
- Adenylosuccinate synthase
- Adenylosuccinate lyase
- reverse
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| IMP→GMP: |
- IMP dehydrogenase
- GMP synthase
- reverse
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|
|
| Nucleotide salvage |
- Hypoxanthine-guanine phosphoribosyltransferase
- Adenine phosphoribosyltransferase
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| Catabolism |
- Adenosine deaminase
- Purine nucleoside phosphorylase
- Guanine deaminase
- Xanthine oxidase
- Urate oxidase
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|
|
| Pyrimidine metabolism |
| Anabolism |
- CAD
- Carbamoyl phosphate synthase II
- Aspartate carbamoyltransferase
- Dihydroorotase
|
|
- Dihydroorotate dehydrogenase
- Orotidine 5'-phosphate decarboxylase/Uridine monophosphate synthetase
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|
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| Catabolism |
- Dihydropyrimidine dehydrogenase
- Dihydropyrimidinase/DPYS
- Beta-ureidopropionase/UPB1
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| Deoxyribonucleotides |
- Ribonucleotide reductase
- Nucleoside-diphosphate kinase
- DCMP deaminase
- Thymidylate synthase
- Dihydrofolate reductase
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Index of inborn errors of metabolism
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| Description |
- Metabolism
- Enzymes and pathways: citric acid cycle
- pentose phosphate
- glycoproteins
- glycosaminoglycans
- phospholipid
- cholesterol and steroid
- sphingolipids
- eicosanoids
- amino acid
- urea cycle
- nucleotide
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|
| Disorders |
- Citric acid cycle and electron transport chain
- Glycoprotein
- Proteoglycan
- Fatty-acid
- Phospholipid
- Cholesterol and steroid
- Eicosanoid
- Amino acid
- Purine-pyrimidine
- Heme metabolism
- Symptoms and signs
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| Treatment |
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UpToDate Contents
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English Journal
- Overexpression, purification, crystallization and preliminary crystallographic studies of a hyperthermophilic adenylosuccinate synthetase from Pyrococcus horikoshii OT3.
- Wang X, Akasaka R, Takemoto C, Morita S, Yamaguchi M, Terada T, Shirozu M, Yokoyama S, Chen S, Si S, Xie Y.SourceInstitute of Medicinal Plants, Chinese Academy of Medical Sciences and Peking Union Medical College, Haidian District, Beijing, People's Republic of China.
- Acta crystallographica. Section F, Structural biology and crystallization communications.Acta Crystallogr Sect F Struct Biol Cryst Commun.2011 Dec 1;67(Pt 12):1551-5. Epub 2011 Nov 25.
- Adenylosuccinate synthetase (AdSS) is a ubiquitous enzyme that catalyzes the first committed step in the conversion of inosine monophosphate (IMP) to adenosine monophosphate (AMP) in the purine-biosynthetic pathway. Although AdSS from the vast majority of organisms is 430-457 amino acids in length,
- PMID 22139164
- The PRPP synthetase spectrum: what does it demonstrate about nucleotide syndromes?
- Duley JA, Christodoulou J, de Brouwer AP.SourceUniversity of Queensland and Mater Medical Research Institute, Brisbane, Australia. jduley@pharmacy.uq.edu.au
- Nucleosides, nucleotides & nucleic acids.Nucleosides Nucleotides Nucleic Acids.2011 Dec;30(12):1129-39.
- Defects in X-linked phosphoribosylpyrophosphate synthetase 1 (PRPS1) manifest as follows: (1) PRS-I enzyme "superactivity" (gain-of-function mutations affecting allosteric regions); (2) PRS-I overexpression (which may be linked to miRNA mutation); (3) severe PRS-I deficiency/Arts syndrome (missense
- PMID 22132967
Japanese Journal
- Differentially expressed proteins in fluconazole-susceptible and fluconazole-resistant isolates of Candida glabrata
- Shen Yinzhong,Zhang Lijun,Jia Xiaofang,Zhang Yongxin,Lu Hongzhou
- Drug Discoveries & Therapeutics 9(3), 191-196, 2015
- … translation elongation factor 3, 3-phosphoglycerate kinase, ribosomal protein L5, coproporphyrinogen III oxidase, pyruvate kinase, G-beta like protein, and F1F0-ATPase alpha subunit were found to be more abundantly represented, while four proteins including vitaminB12-(cobalamin)-independent isozyme of methionine synthase, microtubule-associated protein, adenylosuccinate synthetase, and aldose reductase were found to be less abundantly represented in fluconazole-resistant strains versus those with fluconazole-susceptible …
- NAID 130005088589
Related Links
- 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 ...
★リンクテーブル★
[★]
- 英
- adenylosuccinate synthase
- 関
- アデニロコハク酸シンターゼ
[★]
- 英
- adenylosuccinate synthase
- 関
- アデニロコハク酸合成酵素
[★]
- 関
- lyase、synthetase、transferase