Threo-3-hydroxy-D-aspartate ammonia-lyase

Last updated
Threo-3-hydroxy-D-aspartate ammonia-lyase
Identifiers
EC number 4.3.1.27
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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). [1] This enzyme catalyses the following chemical reaction

threo-3-hydroxy-D-aspartate oxaloacetate + NH3

This enzyme is a pyridoxal-phosphate protein.

Related Research Articles

The urea cycle (also known as the ornithine cycle) is a cycle of biochemical reactions that produces urea (NH2)2CO from ammonia (NH3). This cycle occurs in ureotelic organisms. The urea cycle converts highly toxic ammonia to urea for excretion. This cycle was the first metabolic cycle to be discovered (Hans Krebs and Kurt Henseleit, 1932), five years before the discovery of the TCA cycle. This cycle was described in more detail later on by Ratner and Cohen. The urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.

Serine dehydratase

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 chemical properties vary greatly among species. SDH is found in yeast, bacteria, and the cytoplasm of mammalian hepatocytes. The reaction it 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

In enzymology, an aspartate ammonia-lyase (EC 4.3.1.1) is an enzyme that catalyzes the chemical reaction

In enzymology, a D-serine ammonia-lyase (EC 4.3.1.18) is an enzyme that catalyzes the chemical reaction

In enzymology, an erythro-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.20) is an enzyme that catalyzes the chemical reaction

In enzymology, a glucosaminate ammonia-lyase (EC 4.3.1.9) is an enzyme that catalyzes the chemical reaction

L-serine ammonia-lyase class of enzymes

In enzymology, a L-serine ammonia-lyase (EC 4.3.1.17) is an enzyme that catalyzes the chemical reaction

Methylaspartate ammonia-lyase class of enzymes

In enzymology, a methylaspartate ammonia-lyase (EC 4.3.1.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a threo-3-hydroxyaspartate ammonia-lyase (EC 4.3.1.16) is an enzyme that catalyzes the chemical reaction

In enzymology, a 3-hydroxyaspartate aldolase is an enzyme that catalyzes the chemical reaction

In enzymology, an oxalomalate lyase is an enzyme that catalyzes the chemical reaction

In enzymology, an ATP-dependent NAD(P)H-hydrate dehydratase is an enzyme that catalyzes the chemical reaction

In enzymology, a bile-acid 7alpha-dehydratase (EC 4.2.1.106) is an enzyme that catalyzes the chemical reaction

In enzymology, a D(−)-tartrate dehydratase (EC 4.2.1.81) is an enzyme that catalyzes the chemical reaction

In enzymology, a L(+)-tartrate dehydratase (EC 4.2.1.32) is an enzyme that 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

ADP-dependent NAD(P)H-hydrate dehydratase is an enzyme with systematic name (6S)-6beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine-dinucleotide hydro-lyase . This enzyme catalyses the following chemical reaction

Dihydrodipicolinate synthase class of enzymes

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

References

  1. Maeda T, Takeda Y, Murakami T, Yokota A, Wada M (December 2010). "Purification, characterization and amino acid sequence of a novel enzyme, D-threo-3-hydroxyaspartate dehydratase, from Delftia sp. HT23". Journal of Biochemistry. 148 (6): 705–12. doi:10.1093/jb/mvq106. hdl: 2115/47109 . PMID   20843822.