Reaction participants Show >> << Hide
- Name help_outline N-acetyl-D-phenylalanine Identifier CHEBI:143878 Charge -1 Formula C11H12NO3 InChIKeyhelp_outline CBQJSKKFNMDLON-SNVBAGLBSA-M SMILEShelp_outline C([C@@H](CC1=CC=CC=C1)NC(=O)C)(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-acetyl-L-phenylalanine Identifier CHEBI:57702 (Beilstein: 4189895) help_outline Charge -1 Formula C11H12NO3 InChIKeyhelp_outline CBQJSKKFNMDLON-JTQLQIEISA-M SMILEShelp_outline CC(=O)N[C@@H](Cc1ccccc1)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:62772 | RHEA:62773 | RHEA:62774 | RHEA:62775 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
Related reactions help_outline
More general form(s) of this reaction
Publications
-
Structural basis for catalytic racemization and substrate specificity of an N-acylamino acid racemase homologue from Deinococcus radiodurans.
Wang W.C., Chiu W.C., Hsu S.K., Wu C.L., Chen C.Y., Liu J.S., Hsu W.H.
N-acylamino acid racemase (NAAAR) catalyzes the racemization of N-acylamino acids and can be used in concert with an aminoacylase to produce enantiopure alpha-amino acids, a process that has potential industrial applications. Here we have cloned and characterized an NAAAR homologue from a radiatio ... >> More
N-acylamino acid racemase (NAAAR) catalyzes the racemization of N-acylamino acids and can be used in concert with an aminoacylase to produce enantiopure alpha-amino acids, a process that has potential industrial applications. Here we have cloned and characterized an NAAAR homologue from a radiation-resistant ancient bacterium, Deinococcus radiodurans. The expressed NAAAR racemized various substrates at an optimal temperature of 60 degrees C and had Km values of 24.8 mM and 12.3 mM for N-acetyl-D-methionine and N-acetyl-L-methionine, respectively. The crystal structure of NAAAR was solved to 1.3 A resolution using multiwavelength anomalous dispersion (MAD) methods. The structure consists of a homooctamer in which each subunit has an architecture characteristic of enolases with a capping domain and a (beta/alpha)7 beta barrel domain. The NAAAR.Mg2+ and NAAAR.N-acetyl-L-glutamine.Mg2+ structures were also determined, allowing us to define the Lys170-Asp195-Glu220-Asp245-Lys269 framework for catalyzing 1,1-proton exchange of N-acylamino acids. Four subsites enclosing the substrate are identified: catalytic site, metal-binding site, side-chain-binding region, and a flexible lid region. The high conservation of catalytic and metal-binding sites in different enolases reflects the essentiality of a common catalytic platform, allowing these enzymes to robustly abstract alpha-protons of various carboxylate substrates efficiently. The other subsites involved in substrate recognition are less conserved, suggesting that divergent evolution has led to functionally distinct enzymes. << Less
J. Mol. Biol. 342:155-169(2004) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.