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4.1.3.38 a |
Activity |
4.1.3.38 |
Description |
4-amino-4-deoxychorismate lyase (family a) |
Notes |
A family composed solely of bacterial enzymes, and based on the validated sequences from E. coli and Streptomyces sp. |
PDB |
1ET0; |
PLP Fold Type |
IV |
PLP-dependent Domain |
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Number of sequences |
26 |
Sequences in seed alignment |
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Reference sequence |
PABC_ECOLI |
Domain interval |
37-261 |
Catalytic site |
140 K |
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References |
Chim N, Habel JE, Johnston JM, Krieger I, Miallau L, Sankaranarayanan R, Morse RP, Bruning J, Swanson S, Kim H, Kim CY, Li H, Bulloch EM, Payne RJ, Manos-Turvey A, Hung LW, Baker EN, Lott JS, James MN, Terwilliger TC, Eisenberg DS, Sacchettini JC, Goulding CW. (2011) The TB Structural Genomics Consortium: a decade of progress Tuberculosis (Edinb) 91 155-72. Schadt HS, Schadt S, Oldach F, Süssmuth RD (2009) 2-Amino-2-deoxyisochorismate is a key intermediate in Bacillus subtilis p-aminobenzoic acid biosynthesis. J Am Chem Soc 131 3481-3. Zhang Y, Bai L, Deng Z. (2009) Functional characterization of the first two actinomycete 4-amino-4-deoxychorismate lyase genes Microbiology 155 2450-9. Green, J. M.; Nichols, B. P. (1991) p-Aminobenzoate biosynthesis in Escherichia coli. Purification of aminodeoxychorismate lyase and cloning of pabC J Biol Chem 266 12971-5. Articles on 4.1.3.38.a |
last changed |
2014/02/25 11:18 |
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