Primary structure, sequence analysis, and expression of the thermostable D-hydantoinase from Bacillus stearothermophilus SD1

Molecular and General Genetics

Volumn 255, Issue 2, 1997, Pages 152-156

  Kim, G J ^a   Park, J H ^a   Lee, D C ^a   Ro, H S ^a   Kim, H S ^a  

^a Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

Author keywords

Amidohydrolase; Bacillus stearothermophilus SD1; D hydantoinase

Indexed keywords

ALLANTOIN; BACTERIAL ENZYME; DIHYDROOROTASE; HYDANTOIN; HYDROLASE;

AMINO ACID SEQUENCE; ARTICLE; BIOCHEMISTRY; CARBOXY TERMINAL SEQUENCE; GENETIC CONSERVATION; GEOBACILLUS STEAROTHERMOPHILUS; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; THERMOSTABILITY;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; BACILLUS STEAROTHERMOPHILUS; BASE SEQUENCE; CLONING, MOLECULAR; CONSERVED SEQUENCE; ESCHERICHIA COLI; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SEQUENCE DELETION; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); GEOBACILLUS STEAROTHERMOPHILUS;

EID: 0030871790     PISSN: 00268925     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004380050483     Document Type: Article

References (17)

1. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
2. Buckholz RG, Cooper TG (1991) The allantoinase (DAL1) gene of Saccharomyces cerevisiae. Yeast 7:913-923
3. Jacob E, Henco K, Marcinowski S, Schenk G (1990) Preparation of mesophilic microorganisms which contain a D-hydantoinase which is active at elevated temperature. US Patent Number 4912044
4. Kyte J, Doolitle RF (1982) A simple method for the displaying the hydropathic character of a protein. J Mol Biol 157:105-132
5. Lapointe G, Vian S, Leblanc D, Robert N, Morin A (1994) Cloning, sequencing, and expression in Escherichia coli of the D-hydantoinase gene from Pseudomonas putida and distribution of homologous genes in other microorganisms. Appl Environ Microbiol 60:888-895
6. Lee SG, Lee DC, Hong SP, Sung MH, Kim HS (1995) Thermostable D-hydantoinase from thermophilic Bacillus stearothermophilus SD1: characteristics of purified enzyme. Appl Microbiol Biotechnol 43:270-276
7. Lewington J, Greenaway SD, Spillane BJ (1987) Rapid small-scale preparation of bacterial genomic DNA suitable for cloning and hybridization analysis. Lett Appl Microbiol 5:51-53
8. Miller A, Syldatk C, Schulze M, Wagner F (1988) Stereo- and substrate-specificity of a D-hydantoinase and a N-carbamoyl-D-amino acid amidohydrolase of Arthrobacter crystallopoietes AM2. Enzyme Microb Technol 10:618-625
9. Mukohara Y, Ishikawa T, Watabe K, Nakamura H (1994) A thermostable hydantoinase of Bacillus stearothermophilus NS1122A: cloning, sequencing, and high expression of the enzyme gene, and some properties of the expressed enzyme. Biosci Biotech Biochem 58:1621-1626
10. Sambrook J, Fritsch EF, Maniatis T (1989) Molecular cloning: a laboratory manual (2nd edn). Cold Spring Harbor Laboratory press, Cold Spring Harbor, New York
11. Sanger F, Nickeln S, Coulson AR (1977) DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci USA 74:5463-5467
12. Syldatk C, Laufer A, Muller R, Hoke H (1990) Production of optically pure D-and L-amino acids by bioconversion of D,L-5-monosubstituted hydantoin derivatives. Adv Biochem Eng Biotechnol 41:29-75
13. Vogels GD, Van der Drift C (1976) Degradation of purities and pyrimidines by microorganisms. Bacteriol Rev 40:403-468
14. Watabe K, Ishikawa T, Mukohara Y, Nakamura H (1992) Cloning and sequencing of genes involved in the conversion of 5′-substituted hydantoins to the corresponding L-amino acids from the native plasmid of Pseudomonas up. strain NS671. J Bacteriol 174:962-969
15. Yamada H, Shimizu S (1988) Microbial and enzymatic processes for the production of biologically and chemically useful compounds. Angew Chem Inter Edn 27:622-642
16. Yamashiro A, Kubota K, Yokoseki K (1988) Mechanism of stereospecific production of L-amino acids from the corresponding 5-substituled hydantoins by Bacillus brevis. Agric Biol Chem 52:2857-2863
17. Zimmermann MK, Kemling NM, Evans DR (1995) Function of conserved histidine residues in mammalian dihydroorotase. Biochemistry 34:7038-7046