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2.6.1.72 |
Activity |
2.6.1.72 |
Description |
D-4-hydroxyphenylglycine aminotransferase |
Notes |
The family has been constructed around the validated sequence with this activity, from Pseudomonas stutzeri. |
PDB |
2CY8; |
PLP Fold Type |
I |
PLP-dependent Domain |
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Number of sequences |
7 |
Sequences in seed alignment |
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Reference sequence |
2CY8 |
Domain interval |
42-365 |
Catalytic site |
269 K |
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References |
Walton CJ, Thiebaut F, Brunzelle JS, Couture JF, Chica RA
(2018) Structural determinants of the stereo-inverting activity of Pseudomonas stutzeri D-phenylglycine aminotransferase Biochemistry 57 5437-5446. Chantarasiri A, Meevootisom V, Isarangkul D, Wiyakrutta S.
(2012) Effective improvement of D-phenylglycine aminotransferase solubility by protein crystal contact engineering J Mol Microbiol Biotechnol 22 147-55. Müller U, van Assema F, Gunsior M, Orf S, Kremer S, Schipper D, Wagemans A, Townsend CA, Sonke T, Bovenberg R, Wubbolts M.
(2006) Metabolic engineering of the E. coli L-phenylalanine pathway for the production of D-phenylglycine (D-Phg) Metab Eng 8 196-208. Wiyakrutta S, Meevootisom V. (1997) A stereo-inverting D-phenylglycine aminotransferase from Pseudomonas stutzeri ST-201: purification, characterization and application for D-phenylglycine synthesis J Biotechnol 55 193-203. Articles on 2.6.1.72 |
last changed |
2017/07/24 14:07 |
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