The tyrosine (eTATase) and aspartate (eAATase) aminotransferases of Escherichia coli transaminate diacarboxylic amino acids with similar rate constants. However, eTATase exhibits approximately 10(2)-10(4)-fold higher second-order rate constants for the transamination of aromatic amino acids than doe
Use of Click Chemistry to Define the Substrate Specificity of Leishmania β-1,2-Mannosyltransferases
✍ Scribed by Phillip van der Peet; Carlie T. Gannon; Ian Walker; Zoran Dinev; Marcus Angelin; Shanna Tam; Julie E. Ralton; Malcolm J. McConville; Spencer J. Williams
- Book ID
- 111699005
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- English
- Weight
- 213 KB
- Volume
- 7
- Category
- Article
- ISSN
- 1439-4227
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