| EC |
4.1.3.38 |
| Accepted name: |
aminodeoxychorismate lyase |
| Reaction: |
4-amino-4-deoxychorismate = 4-aminobenzoate + pyruvate |
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For diagram of the late stages of folate biosynthesis, click here |
| Other name(s): |
enzyme X; 4-amino-4-deoxychorismate lyase; 4-amino-4-deoxychorismate pyruvate-lyase |
| Systematic name: |
4-amino-4-deoxychorismate pyruvate-lyase (4-aminobenzoate-forming) |
| Comments: |
A pyridoxal-phosphate protein. Forms part of the folate biosynthesis pathway. Acts on 4-amino-4-deoxychorismate, the product of EC 2.6.1.85, aminodeoxychorismate synthase, to form p-aminobenzoate. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 132264-33-6 |
| References: |
| 1. |
Ye, Q.Z., Liu, J. and Walsh, C.T. p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase. Proc. Natl. Acad. Sci. USA 87 (1990) 9391–9395. [DOI] [PMID: 2251281] |
| 2. |
Green, J.M., Merkel, W.K. and Nichols, B.P. Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme. J. Bacteriol. 174 (1992) 5317–5323. [DOI] [PMID: 1644759] |
| 3. |
Nakai, T., Mizutani, H., Miyahara, I., Hirotsu, K., Takeda, S., Jhee, K.H., Yoshimura, T. and Esaki, N. Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli. J. Biochem. 128 (2000) 29–38. [PMID: 10876155] |
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| [EC 4.1.3.38 created 2003] |
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