Enhanced hydantoin-hydrolyzing enzyme activity in an Agrobacterium tumefaciens strain with two distinct N-carbamoylases

Hydantoin -hydrolyzing enzymes of Agrobacterium tumefaciens isolates such as strain RU-OR are used as biocatalysts in the commercial production of d-hydroxyphenylglycine via hydrolysis of d, l- p-hydroxyphenylhydantoin. Hydantoin-hydrolyzing enzyme activity in RU-OR cells is tightly regulated by nit...

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Bibliographic Details
Published inEnzyme and microbial technology Vol. 44; no. 4; pp. 203 - 209
Main Authors Jiwaji, Meesbah, Hartley, Carol J., Clark, Sally-Ann, Burton, Stephanie G., Dorrington, Rosemary A.
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier Inc 06.04.2009
Elsevier
Subjects
Agrobacterium tumefaciens
Agrobacterium tumefaciens strain RU-OR
Biological and medical sciences
Biotechnology
d- N-Carbamoylase
Enhanced hydantoin hydrolysis
Fundamental and applied biological sciences. Psychology
Enhanced hydantoin hydrolysis
d- N-Carbamoylase
Agrobacterium tumefaciens strain RU-OR
Hydrolysis
o-N-Carbamoylase
Enzymatic activity
Agrobacterium tumefaciens
Bacteria
Rhizobiaceae
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Summary:Hydantoin -hydrolyzing enzymes of Agrobacterium tumefaciens isolates such as strain RU-OR are used as biocatalysts in the commercial production of d-hydroxyphenylglycine via hydrolysis of d, l- p-hydroxyphenylhydantoin. Hydantoin-hydrolyzing enzyme activity in RU-OR cells is tightly regulated by nitrogen catabolite repression and is induced when hydantoin or a hydantoin-analogue is present in the growth medium. Previous studies have selected mutant strains which are inducer-independent and no longer subject to nitrogen catabolite expression. However, these mutants did not exhibit significantly higher levels of enzyme activity compared to the wild-type strain. In this study, we have focused on enhancing the levels of hydantoinase and N-carbamoylase activity in wild-type RU-OR cells by manipulating the growth medium or over-expressing the global nitrogen regulatory factors, NtrBC. We also show that this strain encodes two distinct d-selective N-carbamoylases. One enzyme is virtually identical to the other Agrobacterium N-carbamoylases while the second represents a new class of d- N-carbamoylases with potentially novel biocatalytic properties.
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ISSN:0141-0229
1879-0909
DOI:10.1016/j.enzmictec.2008.11.006