Pfeifer O

References (5)

Title : Cloning of a second non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762: sequence analysis, expression in Streptomyces lividans and enzyme purification - Pelletier_1994_Microbiology_140_509
Author(s) : Pelletier I , Pfeifer O , Altenbuchner J , van Pee KH
Ref : Microbiology , 140 :509 , 1994
Abstract : The gene for BPO-A1, one of two non-haem bromoperoxidases in the tetracycline and 7-chlorotetracycline producer Streptomyces aureofaciens ATCC 10762, was cloned in the positive selection vector pIJ699 and expressed in Streptomyces lividans TK64. The cloned bromoperoxidase was over-produced up to 2800-fold by the S. lividans TK64 transformant. By taking advantage of the over-production of BPO-A1 and the heat stability of the enzyme, a new and simple purification procedure was developed. Subcloning into the vector pIJ487 and screening of recombinants by a newly developed histochemical assay located the bpoA1 gene on a 2.1 kb BamHI-HindIII fragment. The nucleotide sequence of the 2.1 kb fragment was determined; the bpoA1 gene was identified within the sequence on the basis of the biased codon usage of Streptomyces genes and the presence of a nucleotide sequence encoding the N-terminal amino acid sequence obtained from the purified BPO-A1. Comparison of the deduced primary structure of BPO-A1 with those deduced for the non-haem chloroperoxidase CPO-P from Pseudomonas pyrrocinia and the bromoperoxidase BPO-A2 from S. aureofaciens ATCC 10762 gave amino acid sequence identities of 49% and 40%, respectively.
ESTHER : Pelletier_1994_Microbiology_140_509
PubMedSearch : Pelletier_1994_Microbiology_140_509
PubMedID: 8012573
Gene_locus related to this paper: strau-brpa1

Title : The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha\/beta hydrolase fold - Hecht_1994_Nat.Struct.Biol_1_532
Author(s) : Hecht HJ , Sobek H , Haag T , Pfeifer O , van Pee KH
Ref : Nat Struct Biol , 1 :532 , 1994
Abstract : The crystal structure of the bromoperoxidase A2 from Streptomyces aureofaciens (ATCC 10762) has been determined by isomorphous replacement and refined to 2.05 A resolution with an R-value of 18.4%. The enzyme catalyzes the bromination of organic compounds in the presence of bromide and peroxide. The structure confirms the absence of cofactors such as metal ions or haem groups and shows the general topology of the alpha/beta hydrolase fold. The active centre is at the end of a deep pocket and includes a catalytic triad of Ser 98, Asp 228 and His 257. The active centre is connected by a narrow tunnel to a second pocket on the enzyme surface.
ESTHER : Hecht_1994_Nat.Struct.Biol_1_532
PubMedSearch : Hecht_1994_Nat.Struct.Biol_1_532
PubMedID: 7664081
Gene_locus related to this paper: strau-brpa2

Title : Molecular cloning and sequencing of a non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762 - Pfeifer_1992_J.Gen.Microbiol_138_1123
Author(s) : Pfeifer O , Pelletier I , Altenbuchner J , van Pee KH
Ref : J Gen Microbiol , 138 :1123 , 1992
Abstract : A bromoperoxidase gene (bpoT), recently cloned from Streptomyces aureofaciens Tu24, was used as a probe in Southern blot hybridization of total DNA from S. aureofaciens ATCC 10762. A single SstI fragment of 5.4 kb was detected, which was cloned via an enriched gene library into Escherichia coli. The functional bromoperoxidase gene was located on a 2.1 kb BamHI-HindIII fragment by subcloning into S. lividans TK64, using the multicopy plasmid pIJ486. The enzyme was overproduced in S. lividans TK64 (up to 30,000 times compared to S. aureofaciens ATCC 10762) and showed the same electrophoretic and immunological properties as the bromoperoxidase BPO-A2 purified from S. aureofaciens ATCC 10762. DNA sequence analysis revealed an open reading frame encoding a predicted polypeptide with the same M(r) and N-terminal amino acid sequence as the purified subunit of BPO-A2.
ESTHER : Pfeifer_1992_J.Gen.Microbiol_138_1123
PubMedSearch : Pfeifer_1992_J.Gen.Microbiol_138_1123
PubMedID: 1527491
Gene_locus related to this paper: strau-brpa2

Title : Purification, characterization and comparison of two non-haem bromoperoxidases from Streptomyces aureofaciens ATCC 10762 - Weng_1991_J.Gen.Microbiol_137_2539
Author(s) : Weng M , Pfeifer O , Krauss S , Lingens F , van Pee KH
Ref : J Gen Microbiol , 137 :2539 , 1991
Abstract : Two non-haem bromoperoxidases (BPO 1 and BPO 2) were purified from the 7-chlorotetracycline-producing strain Streptomyces aureofaciens ATCC 10762. Both enzymes showed azide-insensitive brominating activity, and bromide-dependent peroxidase activity. BPO 1 was a dimer (Mr 65,000) with subunits of identical size (Mr 31,000). The pI was estimated to be 4.5. The enzyme did not cross-react with antibodies raised against the non-haem bromoperoxidase (Mr 90,000) from S. aureofaciens Tu24, a strain that also produces 7-chlorotetracycline. The Mr of BPO 2 was estimated to be 90,000. The enzyme had three identical subunits (Mr 31,000), and its isoelectric point was 3.5, identical with that of the bromoperoxidase from S. aureofaciens Tu24. Moreover, BPO 2 was immunologically identical with the bromoperoxidase from S. aureofaciens Tu24, although both it and BPO 1 could be distinguished electrophoretically from the latter bromoperoxidase.
ESTHER : Weng_1991_J.Gen.Microbiol_137_2539
PubMedSearch : Weng_1991_J.Gen.Microbiol_137_2539
PubMedID: 1783900
Gene_locus related to this paper: strau-brpa1 , strau-brpa2

Title : Crystallization and preliminary X-ray data of bromoperoxidase from Streptomyces aureofaciens ATCC 10762 - Sobek_1991_J.Mol.Biol_221_35
Author(s) : Sobek H , Haag T , Pfeifer O , Schomburg D , Lingens F , van Pee KH
Ref : Journal of Molecular Biology , 221 :35 , 1991
Abstract : Bromoperoxidase from Streptomyces aureofaciens ATCC 10762, a non-haem haloperoxidase, has been crystallized using the hanging drop method. Preliminary X-ray diffraction studies show that the crystals belong to the cubic space group P2(1)3 with a = 123.4 A. The asymmetric unit contains a dimer of Mr = 60,200. The crystals diffract to at least 2.3 A resolution and are suitable for crystallographic structure analysis.
ESTHER : Sobek_1991_J.Mol.Biol_221_35
PubMedSearch : Sobek_1991_J.Mol.Biol_221_35
PubMedID: 1920414