We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00519Aminotransferases class-III pyridoxal-phosphate attachment site
View entry in original PROSITE document format
View entry in raw text format (no links)
PURL: https://purl.expasy.org/prosite/documentation/PDOC00519
Description
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 α-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 α-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 α-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.
- Bacillus subtilis aminotransferase yhxA.
- Bacillus subtilis aminotransferase yodT.
- Haemophilus influenzae aminotransferase HI0949.
- Caenorhabditis elegans aminotransferase T01B11.2.
The sequence around the pyridoxal-phosphate attachment site of this class of enzyme is sufficiently conserved to allow the creation of a specific pattern.
Last update:December 2004 / Pattern and text revised.
-------------------------------------------------------------------------------
Technical section
PROSITE method (with tools and information) covered by this documentation:
References
| 1 | Authors | Bairoch A. |
| Source | Unpublished observations (1992). |
| 2 | Authors | Yonaha K. Nishie M. Aibara S. |
| Source | J. Biol. Chem. 267:12506-12510(1992). |
Copyright
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.