Characterization and phylogenetic analysis of a thermostable N-carbamoyl-L-amino acid amidohydrolase from Bacillus kaustophilus CCRC11223

Archives of Microbiology

Volumn 179, Issue 4, 2003, Pages 250-257

  Hu, Hui Yu ^a   Hsu, Wen Hwei ^b   Chien, Hungchien Roger ^c  

^a HUNGKUANG UNIVERSITY   (Taiwan)

^b NATIONAL CHUNG HSING UNIVERSITY   (Taiwan)

^c CHUNG SHAN MEDICAL UNIVERSITY   (Taiwan)

Author keywords

Bacillus kaustophilus; N carbamoyl L amino acid amidohydrolase; N carbamoyl L homophenylalanine; Phylogeny; Thermostable enzyme

Indexed keywords

3 AMINO 2 METHYLPROPIONIC ACID; AMIDASE; AMINO ACID DERIVATIVE; BETA ALANINE; COBALT; CYSTEINE DERIVATIVE; MANGANESE; N CARBAMOYLAMINO ACID AMIDOHYDROLASE; N CARBAMOYLHOMOPHENYLALANINE; NICKEL; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; BACILLUS KAUSTOPHILUS; BACTERIAL GENE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME SUBSTRATE; HYDROLYSIS; NUCLEOTIDE SEQUENCE; PH; PHYLOGENY; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; TEMPERATURE DEPENDENCE; THERMOPHILIC BACTERIUM; THERMOSTABILITY;

BACILLUS KAUSTOPHILUS; BACTERIA (MICROORGANISMS); GEOBACILLUS KAUSTOPHILUS; NEGIBACTERIA;

EID: 0037399175     PISSN: 03028933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00203-003-0524-9     Document Type: Article

References (24)

1. Anderson WL, Wetlaufer DB (1975) A new method for disulfide analysis of peptides. Anal Biochem 67:493-502
2. Batisse N, Weigel P, Lecocq M, Sakanyan V (1997) Two amino acid amidohydrolase genes encoding L-stereospecific carbamoylase and aminoacylase are organized in a common operon in Bacillus stearothermophilus. Appl Environ Microbiol 63:763-766
3. Bradford MM (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
4. Burkhard W, Wiese A, Syldatk C, Mattes R, Altenbuchner J, Pietzsch M (1999) Cloning, nucleotide sequence, and expression of a new L-N-carbamoylase gene from Arthrobacter aurescens DSM3747 in E. coli. J Biotechnol 68:101-113
5. Chien HR, Jih Y-L, Yang W-Y, Hsu W-H (1998) Identification of the open reading frame for the Pseudomonas putida D-hydantoinase gene and expression of the gene in Escherichia coli. Biochim Biophy Acta 1395：68-77
6. Doi RH, Rodriques RL, Trait RC (1983) Recombinant DNA techniques: an introduction. Addison-Wesley, Reading, Massachusetts, pp 162-164
7. Ishikawa T, Watabe K, Mukohara Y, Kobayashi S, Nakamura H (1993) Microbial conversion of DL-5-substituted hydanotoins to the corresponding L- amino acids by Pseudomonas sp. strain NS671. Biosci Biotechnol Biochem 57:982-986
8. Ishikawa T, Mukohara Y, Watabe K, Kobayashi S, Nakamura H (1994) Microbial conversion of DL-5-substituted hydantoins to the corresponding L-amino acids by Bacillus stearothermophilus NS 1122A. Biosci Biotechnol Biochem 58:265-270
9. Kieser T (1984) Factors affecting the isolation of cccDNA from Streptomyces lividans and Escherichia coli. Plasmid 12:19-36
10. Kim SS, Choi I-G, Kim S-H, Yu TG (1999) Molecular cloning, expression, and characterization of a thermostable glutamate racemase from a hyperthermophilic bacterium, Aquifex pyrophilus. Extremophiles 3:175-183
11. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
12. Li X, Yeung C-H, Chan ASC, Lee D-S, Yang T-K (1999) An efficient synthesis of chiral homophenylalanine derivatives via enantioselective hydrogenation. Tetrahedron Asymmetry 10:3863-3867
13. Matsumura M, Signor G, Matthews BW (1989) Substantial increase of protein stability by multiple disulphide bonds. Nature 342:291-293
14. May O, Siemann M, Pietzsch M, Kiess M, Mattes R, Syldatk C (1998) Substrate-dependent enantioselectivity of a novel hydantoinase from Arthrobacter aurescens DSM 3745: Purification and characterization as new member of cyclic amidases. J Biotechnol 61:1-13
15. Mukohara Y, Ishikawa T, Watabe K, Nakamura H (1993) Molecular cloning and sequencing of the gene for a thermostable N-carbamoyl-L-amino acid amidohydrolase from Bacillus stearothermophilus strain NS1122A. Biosci Biotechnol Biochem 57:1935-1937
16. Ogawa J, Shimizu S (1994) Ureidopropionase with N-carbamoyl-alpha-L-amino acid amidohydrolase activity from an aerobic bacterium, Pseudomons putida IFO 12996. Eur J Biochem 223:625-630
17. Ogawa J, Miyake H, Shimizu S (1995) Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans. Appl Microbiol Biotechnol 43:1039-1043
18. Sambrook J, Russel DW (2001) Molecular cloning. A laboratory manual, 3rd edn. Cold Spring Harbor Laboratory, Cold Spring Harbor, New York
19. Sears LE, Moran LS, Kissinger C, Creasey T, Perry-O'Keefe H, Roskey M, Sutherland E, Slatko BE (1992) Circum Vent thermal cycle sequencing and alternative manual and automated DNA sequencing protocols using the highly thermostable VentR (exo-) DNA polymerase. BioTech 13:626-633
20. Syldatk C, Cotoras D, Dombach G, Gross C, Kallwass H, Wagner F (1987) Substrate-and stereospecificity, induction and metallo-dependence of a microbial hydantoinase. Biotechnol Lett 9:25-30
21. Watabe K, Ishikawa T, Mukohara Y, Nakamura H (1992) Cloning and sequencing of the genes involved in the conversion of 5-substituted hydantoins to the corresponding L-amino acids from the native plasmid of Pseudomonas sp. strain NS671. J Bacteriol 174:962-969
22. Woese CR, Kandler O, Wheelis ML (1990) Towards a natural system of organisms: proposal for the domains Archaea, Bacteria, and Eukarya. Proc Natl Acad Sci USA 87:4576-4579
23. Yamashiro A, Kubota K, Yokozeki K (1988) Mechanism of stereo-specific production of L-amino acids from the corresponding 5-monosubstituted hydantoins by Bacillus brevis. Agric Biol Chem 52:2857-2863
24. Yokozeki K, Hirose Y, Kubota K (1987) Mechanism of the asymmetric production of L-aromatic amino acids from the corresponding hydantoins by Flavobacterium. Agric Biol Chem 51:737-746