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- * Aminotransferases class-III pyridoxal-phosphate attachment site *
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-
- Aminotransferases share certain mechanistic features with other pyridoxal-
- phosphate dependent enzymes, such as the covalent binding of the pyridoxal-
- phosphate group to a lysine residue. On the basis of sequence similarity,
- these various enzymes can be grouped [1,2] into subfamilies. One of these,
- called class-III, currently consists of the following enzymes:
-
- - Acetylornithine aminotransferase (EC 2.6.1.11) which catalyzes the transfer
- of an amino group from acetylornithine to alpha-ketoglutarate, yielding
- N-acetyl-glutamic-5-semi-aldehyde and glutamic acid.
- - Ornithine aminotransferase (EC 2.6.1.13), which catalyzes the transfer of
- an amino group from ornithine to alpha-ketoglutarate, yielding glutamic-5-
- semi-aldehyde and glutamic acid.
- - Omega-amino acid--pyruvate aminotransferase (EC 2.6.1.18), which catalyzes
- transamination between a variety of omega-amino acids, mono- and diamines,
- and pyruvate. It plays a pivotal role in omega amino acids metabolism.
- - 4-aminobutyrate aminotransferase (EC 2.6.1.19) (GABA transaminase), which
- catalyzes the transfer of an amino group from GABA to alpha-ketoglutarate,
- yielding succinate semialdehyde and glutamic acid.
- - DAPA aminotransferase (EC 2.6.1.62), a bacterial enzyme (gene bioA) which
- catalyzes an intermediate step in the biosynthesis of biotin, the
- transamination of 7-keto-8-aminopelargonic acid (7-KAP) to form 7,8-
- diaminopelargonic acid (DAPA).
- - 2,2-dialkylglycine decarboxylase (EC 4.1.1.64), a Pseudomonas cepacia
- enzyme (gene dgdA) that catalyzes the decarboxylating amino transfer of
- 2,2-dialkylglycine and pyruvate to dialkyl ketone, alanine and carbon
- dioxide.
- - Glutamate-1-semialdehyde aminotransferase (EC 5.4.3.8) (GSA). GSA is the
- enzyme involved in the second step of porphyrin biosynthesis, via the C5
- pathway. It transfers the amino group on carbon 2 of glutamate-1-
- semialdehyde to the neighbouring carbon, to give delta-aminolevulinic acid.
-
- The sequence around the pyridoxal-phosphate attachment site of this class of
- enzyme is sufficiently conserved to allow the creation of a specific pattern.
-
- -Consensus pattern: [LIVMFYW](2)-x-D-E-[LIVMA]-x(2)-[GP]-[LIVMFYWAG]-x(0,1)-
- [ASR]-x-[SAGD]-x(12,16)-D-[LIVMFYW]-x(3)-[SAG]-K-x(3)-
- [STAGN]-[GA]
- [K is the pyridoxal-P attachment site]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
- -Last update: June 1994 / Pattern and text revised.
-
- [ 1] Bairoch A.
- Unpublished observations (1992).
- [ 2] Yonaha K., Nishie M., Aibara S.
- J. Biol. Chem. 267:12506-12510(1992).
-