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Hydantoin racemases substrate specificities

The enzymes of the nucleic acid metabolism are used for several industrial processes. Related to the nucleobase metabolism is the breakdown of hydantoins. The application of these enzymes on a large scale has recently been reviewed [85]. The first step in the breakdown of hydantoins is the hydrolysis of the imide bond. Most of the hydantoinases that catalyse this step are D-selective and they accept many non-natural substrates [78, 86]. The removal of the carbamoyl group can also be catalysed by an enzyme a carbamoylase. The D-selective carbamoylases show wide substrate specificity [85] and their stereoselectivity helps improving the overall enantioselectivity of the process [34, 78, 85]. Genetic modifications have made them industrially applicable [87]. Fortunately hydantoins racemise readily at pH >8 and additionally several racemases are known that can catalyze this process [85, 88]. This means that the hydrolysis of hydantoins is always a dynamic kinetic resolution with yields of up to 100% (Scheme 6.25). Since most hydantoinases are D-selective the industrial application has so far concentrated on D-amino acids. Since 1995 Kaneka Corporation has produced 2000 tons/year of D-p-hydroxyphenylglycine with a D-hydantoinase, a d-carbamoylase [87] and a base-catalysed racemisation [85, 89]. [Pg.282]

The fast and total conversion of i-5-isopropylhydantoin to D-valine by resting microbial cells led Battilotti et al. 0 to the suggestion that a hydantoin racemase might be responsible for the racemization of the L-enantiomer. The first hydantoin racemase to be described in detail was a 5-arylalkylhydantoin racemase, which was isolated and purified from Arthrobacter sp. DSM 3747155, 144> 145l. Its substrate specificity is shown in Fig. 12.4-21. [Pg.793]

Figure 12.4-21. Substrate specificity of the hydantoin racemase from Arthrobacter sp. DSM 3745 55 1441... Figure 12.4-21. Substrate specificity of the hydantoin racemase from Arthrobacter sp. DSM 3745 55 1441...
In many cases, the racemization of a substrate required for DKR is difficult As an example, the production of optically pure cc-amino acids, which are used as intermediates for pharmaceuticals, cosmetics, and as chiral synfhons in organic chemistry [31], may be discussed. One of the important methods of the synthesis of amino acids is the hydrolysis of the appropriate hydantoins. Racemic 5-substituted hydantoins 15 are easily available from aldehydes using a commonly known synthetic procedure (Scheme 5.10) [32]. In the next step, they are enantioselectively hydrolyzed by d- or L-specific hydantoinase and the resulting N-carbamoyl amino acids 16 are hydrolyzed to optically pure a-amino acid 17 by other enzymes, namely, L- or D-specific carbamoylase. This process was introduced in the 1970s for the production of L-amino acids 17 [33]. For many substrates, the racemization process is too slow and in order to increase its rate enzymes called racemases are used. In processes the three enzymes, racemase, hydantoinase, and carbamoylase, can be used simultaneously this enables the production of a-amino acids without isolation of intermediates and increases the yield and productivity. Unfortunately, the commercial application of this process is limited because it is based on L-selective hydantoin-hydrolyzing enzymes [34, 35]. For production of D-amino acid the enzymes of opposite stereoselectivity are required. A recent study indicates that the inversion of enantioselectivity of hydantoinase, the key enzyme in the... [Pg.103]


See other pages where Hydantoin racemases substrate specificities is mentioned: [Pg.223]    [Pg.63]    [Pg.762]    [Pg.765]    [Pg.168]    [Pg.393]    [Pg.11]    [Pg.12]    [Pg.86]    [Pg.132]   
See also in sourсe #XX -- [ Pg.12 ]




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