| threo-3-hydroxyaspartate ammonia-lyase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.3.1.16 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) is an enzyme that catalyzes the chemical reaction
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is threo-3-hydroxy-L-aspartate ammonia-lyase (oxaloacetate-forming). Other names in common use include threo-3-hydroxyaspartate dehydratase, L-threo-3-hydroxyaspartate dehydratase, and threo-3-hydroxy-L-aspartate ammonia-lyase.
The urea cycle (also known as the ornithine cycle) is a cycle of biochemical reactions that produces urea (NH2)2CO from ammonia (NH3). Animals that use this cycle, mainly amphibians and mammals, are called ureotelic.
Serine dehydratase or L-serine ammonia lyase (SDH) is in the β-family of pyridoxal phosphate-dependent (PLP) enzymes. SDH is found widely in nature, but its structural and properties vary among species. SDH is found in yeast, bacteria, and the cytoplasm of mammalian hepatocytes. SDH catalyzes is the deamination of L-serine to yield pyruvate, with the release of ammonia.
Aspartate dehydrogenase (EC 1.4.1.21) is an enzyme that catalyzes the chemical reaction
The enzyme aspartate ammonia-lyase (EC 4.3.1.1) catalyzes the chemical reaction
The enzyme D-serine ammonia-lyase (EC 4.3.1.18), with systematic name D-serine ammonia-lyase (pyruvate-forming), catalyzes the chemical reaction
The enzyme erythro-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.20) catalyzes the chemical reaction
The enzyme Glucosaminate ammonia-lyase (EC 4.3.1.9) catalyzes the chemical reaction
The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction
The enzyme methylaspartate ammonia-lyase (EC 4.3.1.2) catalyzes the chemical reaction
The enzyme L-erythro-3-hydroxyaspartate aldolase catalyzes the chemical reaction
The enzyme 4a-hydroxytetrahydrobiopterin dehydratase (EC 4.2.1.96) catalyzes the chemical reaction
The enzyme ATP-dependent NAD(P)H-hydrate dehydratase catalyzes the chemical reactions
The enzyme D(−)-tartrate dehydratase (EC 4.2.1.81) catalyzes the chemical reaction
The enzyme L(+)-tartrate dehydratase (EC 4.2.1.32) catalyzes the chemical reaction
The enzyme trans-L-3-hydroxyproline dehydratase (EC 4.2.1.77) catalyzes the chemical reaction
3-hydroxy-D-aspartate aldolase is an enzyme with systematic name 3-hydroxy-D-aspartate glyoxylate-lyase (glycine-forming). This enzyme catalyses the following chemical reaction
Aldos-2-ulose dehydratase (EC 4.2.1.110, pyranosone dehydratase, AUDH, 1,5-anhydro-D-fructose dehydratase (microthecin-forming)) is an enzyme with systematic name 1,5-anhydro-D-fructose hydro-lyase (microthecin-forming). This enzyme catalyses the following chemical reaction
threo-3-Hydroxy-D-aspartate ammonia-lyase (EC 4.3.1.27, D-threo-3-hydroxyaspartate dehydratase) is an enzyme with systematic name threo-3-hydroxy-D-aspartate ammonia-lyase (oxaloacetate-forming). This enzyme catalyses the following chemical reaction
4-Hydroxy-tetrahydrodipicolinate synthase (EC 4.3.3.7, dihydrodipicolinate synthase, dihydropicolinate synthetase, dihydrodipicolinic acid synthase, L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing), dapA (gene)) is an enzyme with the systematic name L-aspartate-4-semialdehyde hydro-lyase (adding pyruvate and cyclizing; (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate-forming). This enzyme catalyses the following chemical reaction
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