Expression and characterization of a second L-amino acid deaminase isolated from Proteus mirabilis in Escherichia coli
DC Field | Value | Language |
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dc.contributor.author | Baek, Jin-Oh | - |
dc.contributor.author | Seo, Jeong-Woo | - |
dc.contributor.author | Kwon, Ohsuk | - |
dc.contributor.author | Seong, Su-Il | - |
dc.contributor.author | Kim, Ik-Hwan | - |
dc.contributor.author | Kim, Chul Ho | - |
dc.date.accessioned | 2021-09-07T13:39:27Z | - |
dc.date.available | 2021-09-07T13:39:27Z | - |
dc.date.created | 2021-06-14 | - |
dc.date.issued | 2011-04 | - |
dc.identifier.issn | 0233-111X | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/112747 | - |
dc.description.abstract | L-amino acid deaminases catalyze the deamination of natural L-amino acids. Two types of L-amino acid deaminase have been identified in Proteus species. One exhibits high levels of activity toward a wide range of aliphatic and aromatic L-amino acids, typically L-phenylalanine, whereas the other acts on a relatively narrow range of basic L-amino acids, typically L-histidine. In this study, we cloned, expressed, and characterized a second amino acid deaminase, termed Pm1, from P. mirabilis KCTC 2566. Homology alignment of the deduced amino acid sequence of Pm1 demonstrated that the greatest similarity (96%) was with the L-amino acid deaminase (LAD) of P. vulgaris, and that homology with Pma was relatively low (72%). Also, similar to LAD, Pm1 was most active on L-histidine, indicating that Pm1 belongs to the second type of amino acid deaminase. In agreement with this conclusion, the V(max) and K(m) values of Pm1 were 119.7 (mu g phenylpyruvic acid/mg/min) and 31.55 mM phenylalanine, respectively, values lower than those of Pma. The Pm1 deaminase will be very useful industrially in the preparation of commercially valuable materials including urocanic acid and a-oxoglutarate. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | WILEY-BLACKWELL | - |
dc.subject | RHODOCOCCUS-OPACUS | - |
dc.subject | PHENYLLACTIC ACID | - |
dc.subject | SEQUENCE | - |
dc.subject | PURIFICATION | - |
dc.subject | OXIDASES | - |
dc.subject | METABOLISM | - |
dc.subject | MECHANISM | - |
dc.subject | SUBSTRATE | - |
dc.subject | HISTIDINE | - |
dc.subject | VULGARIS | - |
dc.title | Expression and characterization of a second L-amino acid deaminase isolated from Proteus mirabilis in Escherichia coli | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Ik-Hwan | - |
dc.identifier.doi | 10.1002/jobm.201000086 | - |
dc.identifier.scopusid | 2-s2.0-79954545667 | - |
dc.identifier.wosid | 000290445900002 | - |
dc.identifier.bibliographicCitation | JOURNAL OF BASIC MICROBIOLOGY, v.51, no.2, pp.129 - 135 | - |
dc.relation.isPartOf | JOURNAL OF BASIC MICROBIOLOGY | - |
dc.citation.title | JOURNAL OF BASIC MICROBIOLOGY | - |
dc.citation.volume | 51 | - |
dc.citation.number | 2 | - |
dc.citation.startPage | 129 | - |
dc.citation.endPage | 135 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Microbiology | - |
dc.relation.journalWebOfScienceCategory | Microbiology | - |
dc.subject.keywordPlus | RHODOCOCCUS-OPACUS | - |
dc.subject.keywordPlus | PHENYLLACTIC ACID | - |
dc.subject.keywordPlus | SEQUENCE | - |
dc.subject.keywordPlus | PURIFICATION | - |
dc.subject.keywordPlus | OXIDASES | - |
dc.subject.keywordPlus | METABOLISM | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | SUBSTRATE | - |
dc.subject.keywordPlus | HISTIDINE | - |
dc.subject.keywordPlus | VULGARIS | - |
dc.subject.keywordAuthor | Proteus mirabilis | - |
dc.subject.keywordAuthor | Amino acid deaminase | - |
dc.subject.keywordAuthor | Phenylpyruvic acid | - |
dc.subject.keywordAuthor | Phenyllactic acid | - |
dc.subject.keywordAuthor | Ferric chloride | - |
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