Properties of α-Amino-ε-caprolactam Racemase from<i>Achromobacter obae</i>

Ahmed, Salman; Esaki, Nobuyoshi; Tanaka, Hidehiko; Soda, Kenji

doi:10.1080/00021369.1983.10865864

Cited by 7 publications

(16 citation statements)

References 8 publications

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“…[82,85] 3.3.1.2 The Enzyme a-Amino-e-amino-caprolactam racemase is a monomer with an approximate molecular weight of 49 ± 51 kDa. [82,86] Similar to other amino acid racemases described above, PLP is required as cofactor for activity. Although a one-base mechanism has been proposed, [86] details on the mechanism or the enzyme×s structure are not yet available.…”

Section: Racemisation Of A-amino Lactamsmentioning

confidence: 75%

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Enzymatic Racemisation and its Application to Synthetic Biotransformations

2003

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Section: Racemisation Of A-amino Lactamsmentioning

confidence: 75%

“…[82,86] Similar to other amino acid racemases described above, PLP is required as cofactor for activity. Although a one-base mechanism has been proposed, [86] details on the mechanism or the enzyme×s structure are not yet available.…”

Section: Racemisation Of A-amino Lactamsmentioning

confidence: 75%

Enzymatic Racemisation and its Application to Synthetic Biotransformations

2003

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“…l. -) is unique among racemases in acting ex elusively on ACL and a-amino-5-valerolactam. Recently, Ahmed et al stud ied the mechanism of ACL racemase (190). The enzyme catalyzes exchange of the a-hyrogen of the substrate with deuterium or tritium during racemiza tion in deuterium oxide or tritiated water (191).…”

Section: A-amino'-e-caprolactam (Acl) Racemasementioning

confidence: 99%

Recent Topics in Pyridoxal 5'-Phosphate Enzyme Studies

Hayashi¹,

Wada²,

Yoshimura³

et al. 1990

Annu. Rev. Biochem.

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“…However, detailed properties of ACL racemase were studied only with ACL racemase from A. obae [14][15][16][17][18][19]. This enzyme was used in combination with L-ACL hydrolase from Cryptococcus laurentii, Candida humicola, or Trichosporon cutaneum for L-lysine production from D-and L-ACL on an industrial scale [20,21].…”

Section: Introductionmentioning

confidence: 99%

In Silico Identification for α-Amino-ε-Caprolactam Racemases by Using Information on the Structure and Function Relationship

Payoungkiattikun

Okazaki

Nakano

et al. 2015

Appl Biochem Biotechnol

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In silico identification for enzymes having desired functions is attractive because there is a possibility that numerous desirable enzymes have been deposited in databases. In this study, α-amino-ε-caprolactam (ACL) racemases were searched from the NCBI protein database. Four hundred thirteen fold-type I pyridoxal 5'-phosphate-dependent enzymes which are considered to contain sequences of ACL racemase were firstly obtained by submitting the sequence of ACL racemase from Achromobacter obae to the database. By identifying Lys241 as a key amino acid residue, 13 candidates for ACL racemase were selected. Then, putative ACL racemase genes were synthesized as codon-optimized sequences for expression in Escherichia coli. They were subcloned and expressed in E. coli BL21 and underwent His-tag purification. ACL and amino acid amide racemizing activities were detected among ten of the candidates. The locus tags Oant_4493, Smed_5339, and CSE45_2055 derived from Ochrobactrum anthropi ATCC49188, Sinorhizobium medicae WSM 419, and Citreicella sp. SE45, respectively, showed higher racemization activity against D- and L-ACLs rather than that of ACL racemase from A. obae. Our results demonstrate that the newly discovered ACL racemases were unique from ACL racemase from A. obae and might be useful for applications in dynamic kinetic resolution for D- or L-amino acid production.

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Properties of α-Amino-ε-caprolactam Racemase fromAchromobacter obae

Cited by 7 publications

References 8 publications

Enzymatic Racemisation and its Application to Synthetic Biotransformations

Enzymatic Racemisation and its Application to Synthetic Biotransformations

Recent Topics in Pyridoxal 5'-Phosphate Enzyme Studies

In Silico Identification for α-Amino-ε-Caprolactam Racemases by Using Information on the Structure and Function Relationship

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