Literature DB >> 7764340

Molecular cloning and sequencing of the gene for a thermostable N-carbamyl-L-amino acid amidohydrolase from Bacillus stearothermophilus strain NS1122A.

Y Mukohara1, T Ishikawa, K Watabe, H Nakamura.   

Abstract

The gene for N-carbamyl-L-amino acid amidohydrolase was cloned from Bacillus stearothermophilus strain NS1122A into E. coli. This gene started with a TTG triplet and was predicted to encode a peptide of 409 amino acids, with a calculated molecular weight of 44,248. The deduced amino acid sequence shared moderate homology with that of the corresponding enzyme of Pseudomonas sp. strain NS671.

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Year:  1993        PMID: 7764340     DOI: 10.1271/bbb.57.1935

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  3 in total

1.  Two amino acid amidohydrolase genes encoding L-stereospecific carbamoylase and aminoacylase are organized in a common operon in Bacillus stearothermophilus.

Authors:  N Batisse; P Weigel; M Lecocq; V Sakanyan
Journal:  Appl Environ Microbiol       Date:  1997-02       Impact factor: 4.792

2.  Genes from Pseudomonas sp. strain BS involved in the conversion of L-2-amino-Delta(2)-thiazolin-4-carbonic acid to L-cysteine.

Authors:  Toshikazu Shiba; Kohji Takeda; Misako Yajima; Makoto Tadano
Journal:  Appl Environ Microbiol       Date:  2002-05       Impact factor: 4.792

3.  Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans.

Authors:  J Ogawa; H Miyake; S Shimizu
Journal:  Appl Microbiol Biotechnol       Date:  1995-11       Impact factor: 4.813

  3 in total

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