| EC |
4.1.1.45 |
| Accepted name: |
aminocarboxymuconate-semialdehyde decarboxylase |
| Reaction: |
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO2 |
|
For diagram of the later stages of tryptophan catabolism, click here |
| Glossary: |
aminocarboxymuconate semialdehyde = 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate |
| Other name(s): |
picolinic acid carboxylase; picolinic acid decarboxylase; α-amino-β-carboxymuconate-ε-semialdehade decarboxylase; α-amino-β-carboxymuconate-ε-semialdehyde β-decarboxylase; 2-amino-3-(3-oxoprop-2-enyl)but-2-enedioate carboxy-lyase; 2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase |
| Systematic name: |
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate carboxy-lyase (2-aminomuconate-semialdehyde-forming) |
| Comments: |
Product rearranges non-enzymically to picolinate. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37289-47-7 |
| References: |
| 1. |
Ichiyama, A., Nakamura, S., Kawai, H., Honjo, T., Nishizuka, Y., Hayaishi, O. and Senoh, S. Studies on the metabolism of the benzene ring of tryptophan in mammalian tissues. II. Enzymic formation of α-aminomuconic acid from 3-hydroxyanthranilic acid. J. Biol. Chem. 240 (1965) 740–749. [PMID: 14275130] |
|
| [EC 4.1.1.45 created 1972] |
| |
|
| |
|
Printable version