WordNet
- a pungent gas compounded of nitrogen and hydrogen (NH3)
PrepTutorEJDIC
- アンモニア / アンモニア水(ammonia water)
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/12/12 05:29:11」(JST)
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| aspartate ammonia-lyase |
| Identifiers |
| EC number |
4.3.1.1 |
| CAS number |
9027-30-9 |
| 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 / QuickGO |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
|
In enzymology, an aspartate ammonia-lyase (EC 4.3.1.1) is an enzyme that catalyzes the chemical reaction
- L-aspartate fumarate + NH3
Hence, this enzyme has one substrate, L-aspartate, and two products, fumarate and NH3.
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is L-aspartate ammonia-lyase (fumarate-forming). Other names in common use include aspartase, fumaric aminase, L-aspartase, and L-aspartate ammonia-lyase. This enzyme participates in alanine and aspartate metabolism and nitrogen metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1J3U and 1JSW.
References
- Ellfolk N; Kjærgård, T.; Bánhidi, Z. G.; Virtanen, Artturi I.; Sörensen, Nils Andreas (1953). "Studies on aspartase. 1. Quantitative separation of aspartase from bacterial cells, and its partial purification". Acta Chem. Scand. 7: 824–830. doi:10.3891/acta.chem.scand.07-0824.
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Carbon-nitrogen lyases (EC 4.3)
|
| 4.3.1: ammonia-lyases |
- Histidine ammonia-lyase
- Formiminotransferase cyclodeaminase
- Serine dehydratase
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| 4.3.2: amidine-lyases |
- Argininosuccinate lyase
- Adenylosuccinate lyase
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Enzymes
|
| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
|
| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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| Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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| Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
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UpToDate Contents
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Japanese Journal
- Evaluation of functionally important amino acids in L-aspartate ammonia-lyase from Escherichia coli.
- The structure of L-aspartate ammonia-lyase from Escherichia coli.
Related Links
- cytosol, membrane, aspartate ammonia-lyase activity, aspartate metabolic process, cellular amino acid biosynthetic process, protein tetramerization ... « Hide 10 20 30 40 50 MSNNIRIEED LLGTREVPAD ...
- cytosol, aspartate ammonia-lyase activity, aspartate metabolic process, cellular amino acid biosynthetic process, protein tetramerization ... « Hide 10 20 30 40 50 MLNGQKEYRV EKDFLGEKQI EADVYYGIQT ...
Related Pictures
★リンクテーブル★
[★]
- 英
- aspartate ammonia-lyase
[★]
アスパラギン酸、アスパラギン酸塩
- 関
- Asp、aspartic、aspartic acid、D、L-aspartate、L-aspartic acid、magnesium aspartate、potassium aspartate
- aspartic acid
[★]
アンモニア NH3