ID: | 4.1.3.38 |
---|---|
Description: | Aminodeoxychorismate lyase. |
Alternative Name: |
Enzyme X. ADC lyase. 4-amino-4-deoxychorismate pyruvate-lyase. 4-amino-4-deoxychorismate lyase. |
Cath: | 3.20.10.10; 3.30.470.10; 3.60.120.10; |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 4.1.3.38 |
BRENDA Enzyme Link: | BRENDA 4.1.3.38 |
KEGG Enzyme Link: | KEGG4.1.3.38 |
BioCyc Enzyme Link: | BioCyc 4.1.3.38 |
ExPASy Enzyme Link: | ExPASy4.1.3.38 |
EC2PDB Enzyme Link: | EC2PDB 4.1.3.38 |
ExplorEnz Enzyme Link: | ExplorEnz 4.1.3.38 |
PRIAM enzyme-specific profiles Link: | PRIAM 4.1.3.38 |
IntEnz Enzyme Link: | IntEnz 4.1.3.38 |
MEDLINE Enzyme Link: | MEDLINE 4.1.3.38 |
RHEA:16201 | 4-amino-4-deoxychorismate = 4-aminobenzoate + H(+) + pyruvate |
RULE(radius=1) | [*:1]-[CH;+0:2]1-[CH;+0:3]=[CH;+0:4]-[C;H0;+0:5](-[*:6])=[CH;+0:7]-[CH;+0:8]-1-[O;H0;+0:9]-[C;H0;+0:10](-[*:11])=[CH2;+0:12]>>[*:11]-[C;H0;+0:10](-[CH3;+0:12])=[O;H0;+0:9].[*:1]-[c;H0;+0:2]1:[cH;+0:3]:[cH;+0:4]:[c;H0;+0:5](-[*:6]):[cH;+0:7]:[cH;+0:8]:1 |
Reaction | ![]() |
Core-to-Core |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Characterization and sequence of Escherichia coli pabC, the gene encoding aminodeoxychorismate lyase, a pyridoxal phosphate-containing enzyme. | Green JM, Merkel WK, Nichols BP | 1992 Aug | 1644759 |
Three-dimensional structure of 4-amino-4-deoxychorismate lyase from Escherichia coli. | Nakai T, Mizutani H, Miyahara I, Hirotsu K, Takeda S, Jhee KH, Yoshimura T, Esaki N | 2000 Jul | 10876155 |