Cloning, nucleotide sequence and expression of a new --carbamoylase gene from DSM 3747 in

Wilms, Burkhard; Wiese, Anja; Syldatk, Christoph; Mattes, Ralf; Altenbuchner, Josef; Pietzsch, Markus

doi:10.1016/s0168-1656(98)00183-7

Cited by 40 publications

(38 citation statements)

References 28 publications

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“…A computer-aided homology search using the FASTA program (10) revealed that ORF2 is homologous with Ncarbamoyl-L-amino acid amidohydrolases (L-N-carbamoylase), including N-carbamoyl-␤-alanine amidohydrolase, from Arthrobacter aurescens (23), Bacillus stearothermophilus (2, 9), Pseudomonas sp. NS671 (22), and Saccharomyces kluyveri (Z. Gojkovic, M. Sandrini, and J. Piskur, unpublished results [GenBank accession number AF333185]).…”

Section: Resultsmentioning

confidence: 99%

“…The homologue also has L-ATC hydrolase activity, and its amino acid sequence is 53.5% identical with AtcB (1). L-NCC amidohydrolase encoded by atcC shares strong homology with L-N-carbamoylase (23). L-N-Carbamoylase catalyzes the conversion of N-carbamyl-L-amino acids to L-amino acids (23).…”

Section: Discussionmentioning

confidence: 99%

“…L-NCC amidohydrolase encoded by atcC shares strong homology with L-N-carbamoylase (23). L-N-Carbamoylase catalyzes the conversion of N-carbamyl-L-amino acids to L-amino acids (23). The gene for L-N-carbamoylase has been cloned in Pseudomonas sp.…”

Section: Discussionmentioning

confidence: 99%

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Genes from Pseudomonas sp. Strain BS Involved in the Conversion of l -2-Amino-Δ ² -Thiazolin-4-Carbonic Acid to l -Cysteine

Shiba

Takeda

Yajima

et al. 2002

Appl Environ Microbiol

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DL-2-amino-⌬2 -thiazolin-4-carbonic acid (DL-ATC) is a substrate for cysteine synthesis in some bacteria, and this bioconversion has been utilized for cysteine production in industry. We cloned a DNA fragment containing the genes involved in the conversion of L-ATC to L-cysteine from Pseudomonas sp. strain BS. The introduction of this DNA fragment into Escherichia coli cells enabled them to convert L-ATC to cysteine via N-carbamyl-Lcysteine (L-NCC) as an intermediate. The smallest recombinant plasmid, designated pTK10, contained a 2.6-kb insert DNA fragment that has L-cysteine synthetic activity. The nucleotide sequence of the insert DNA revealed that two open reading frames (ORFs) encoding proteins with molecular masses of 19.5 and 44.7 kDa were involved in the L-cysteine synthesis from DL-ATC. These ORFs were designated atcB and atcC, respectively, and their gene products were identified by overproduction of proteins encoded in each ORF and by the maxicell method. The functions of these gene products were examined using extracts of E. coli cells carrying deletion derivatives of pTK10. The results indicate that atcB and atcC are involved in the conversion of L-ATC to L-NCC and the conversion of L-NCC to cysteine, respectively. atcB was first identified as a gene encoding an enzyme that catalyzes thiazolin ring opening. AtcC is highly homologous with L-N-carbamoylases. Since both enzymes can only catalyze the L-specific conversion from L-ATC to L-NCC or L-NCC to L-cysteine, it is thought that atcB and atcC encode L-ATC hydrolase and N-carbamyl-L-cysteine amidohydrolase, respectively.L-cysteine has been widely used in medicines, cosmetics, and food additives. It has mainly been produced via acid or alkaline hydrolysis of human and animal hairs. However, these methods result in low yields and give rise to unpleasant odors and problems of waste treatment (11). In addition, products extracted from hair do not qualify for medical use because of sanitary problems.A bioconversion, instead of hydrolysis of hairs, for producing L-cysteine has also been developed (14,15). Some bacteria, especially in the genus Pseudomonas (14, 15, 21), have potent activities of asymmetrical hydrolysis of DL-2-amino-⌬ 2 -thiazolin-4-carbonic acid (DL-ATC) to form L-cysteine. DL-ATC is a desirable substrate for the bioconversion since the method for chemical synthesis of DL-ATC is not complicated (14, 15). The total cost for L-cysteine synthesis using DL-ATC is favorable for the large-scale production in industry because the price of DL-ATC is less than that of L-cysteine. Cultured bacteria have been used for commercial production of L-cysteine. As summarized in Fig. 1, bacterial conversion of DL-ATC to L-cysteine consists of the following three successive steps (21): (i) enzymatic racemization of D-ATC to L-ATC; (ii) a ring-opening hydrolysis of L-ATC with an enzyme called ATC hydrolase, to produce either N-carbamyl-L-cysteine (L-NCC) or S-carbamyl-L-cysteine (L-SCC) as intermediates; and (iii) hydrolysis of these intermediates to L-cystei...

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Genes from Pseudomonas sp. Strain BS Involved in the Conversion of l -2-Amino-Δ ² -Thiazolin-4-Carbonic Acid to l -Cysteine

Shiba

Takeda

Yajima

et al. 2002

Appl Environ Microbiol

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“…18,22,23) Several microorganisms producing N-carbamoyl-D-and W or N-carbamoyl-Lamino acid amidohydrolases have been isolated, and some of these enzymes were puriˆed and characterized. 16,19,21,[24][25][26] These results suggest that there are 2 classes of N-carbamoyl amino acid amidohydrolases, N-carbamoyl-D-and N-carbamoyl-L-amino acid amidohydrolases. NCC amidohydrolase hydrolyzed only the L-form of NCC, 5) and showed signiˆcant similarity to the known N-carbamoyl-L-amino acid amidohydrolases (Fig.…”

mentioning

confidence: 81%

“…These are the enzymes from A. aurescence DSM3747, 16) B. stearothermophilus NS714A, 17) Pseudomonas sp. NS671, 18) B. subtilis (GenBank accession number Z99120), E. coli (U82664), and H. in‰uenzae (U32740).…”

Section: Identiˆcation Of Atc Hydrolase and Ncc Amidohydrolasementioning

confidence: 99%

Identification, Cloning, and Sequencing of the Genes Involved in the Conversion ofD,L-2-Amino-Δ²-Thiazoline-4-Carboxylic Acid to …

Ohmachi¹,

Nishino²,

Kawata³

et al. 2002

Bioscience, Biotechnology, and Biochemistry

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Hydrolysis and Formation of Hydantoins

Pietzsch¹,

Syldatk²

2002

Enzyme Catalysis in Organic Synthesis

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Cloning, nucleotide sequence and expression of a new --carbamoylase gene from DSM 3747 in

Cited by 40 publications

References 28 publications

Genes from Pseudomonas sp. Strain BS Involved in the Conversion of l -2-Amino-Δ ² -Thiazolin-4-Carbonic Acid to l -Cysteine

Genes from Pseudomonas sp. Strain BS Involved in the Conversion of l -2-Amino-Δ ² -Thiazolin-4-Carbonic Acid to l -Cysteine

Identification, Cloning, and Sequencing of the Genes Involved in the Conversion ofD,L-2-Amino-Δ²-Thiazoline-4-Carboxylic Acid to …

Hydrolysis and Formation of Hydantoins

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Cloning, nucleotide sequence and expression of a new --carbamoylase gene from DSM 3747 in

Cited by 40 publications

References 28 publications

Genes from Pseudomonas sp. Strain BS Involved in the Conversion of l -2-Amino-Δ 2 -Thiazolin-4-Carbonic Acid to l -Cysteine

Genes from Pseudomonas sp. Strain BS Involved in the Conversion of l -2-Amino-Δ 2 -Thiazolin-4-Carbonic Acid to l -Cysteine

Identification, Cloning, and Sequencing of the Genes Involved in the Conversion ofD,L-2-Amino-Δ2-Thiazoline-4-Carboxylic Acid to …

Hydrolysis and Formation of Hydantoins

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Genes from Pseudomonas sp. Strain BS Involved in the Conversion of l -2-Amino-Δ ² -Thiazolin-4-Carbonic Acid to l -Cysteine

Genes from Pseudomonas sp. Strain BS Involved in the Conversion of l -2-Amino-Δ ² -Thiazolin-4-Carbonic Acid to l -Cysteine

Identification, Cloning, and Sequencing of the Genes Involved in the Conversion ofD,L-2-Amino-Δ²-Thiazoline-4-Carboxylic Acid to …