Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:1.9.3.1 (
cytochrome oxidase
)
8,822
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The gene coding for cytochrome oxidase subunit I (COI) was isolated from a genomic DNA library of the thermophilic bacterium PS3 and sequenced. The N-terminal of the
COI protein
was also sequenced to verify the initiation site of the reading frame. The deduced amino acid sequence of
COI protein
is composed of 536 amino acid residues and its molecular mass is 59,510. The protein is clearly homologous to the corresponding subunit in the mitochondrial
cytochrome oxidase
and similarly appears to have 12 trans-membrane segments. The proposed ligands to two hemes (
cytochrome aa3
) and a copper atom (CuB) in this protein (Holm et al. (1987) EMBO J. 6, 2819-2823) are conserved in the sequence.
...
PMID:Nucleotide sequence of the gene coding for cytochrome oxidase subunit I from the thermophilic bacterium PS3. 284 37
The gene (coxI or CoxA) encoding subunit I (COI) of
cytochrome-c oxidase
(
cytochrome aa3
) of Synechocystis PCC6803, Synechococcus PCC7942 (Anacystis nidulans R2) and Nostoc PCC8002 (Nostoc Mac), was identified by heterologous hybridization of chromosomal digests with a 17-bp oligodeoxyribonucleotide (probe C) derived from the coxI of Paracoccus denitrificans. A single genomic fragment was found to bind to probe C in all chromosomal digests. Due to its favorable signal-to-noise ratio, the genome of Synechocystis was chosen for the isolation and sequencing of this gene. A genomic DNA library in pUC18 was screened with probe C. The two probe C-positive plasmids, pDAUV1 and pDAUV2, contained a 1-kb overlapping region, with the conserved 17-bp sequence encoding the CuB-binding region of the COI polypeptide. These plasmids were subcloned into competent Escherichia coli DH5 alpha cells, and the nucleotide sequences were determined. The deduced amino acid (aa) sequences of Synechocystis COI and homologous proteins from a variety of prokaryotic and eukaryotic organisms showed an overall similarity of between 38.6 and 45.8%. Hydropathy plots revealed 12 potential transmembrane helices. All of the six histidines needed for the binding of heme a and the heme a3/CuB bimetallic center are present in the expected positions of the Synechocystis
COI protein
(533 aa, M(r) 59,390). A monospecific antibody raised against P. denitrificans COI gave an unequivocal immunological cross-reaction on Western blots of membrane preparations from Synechocystis, Anacystis and Nostoc, showing that the product of gene coxI is indeed synthesized and incorporated into cyanobacterial membranes.
...
PMID:The gene encoding cytochrome-c oxidase subunit I from Synechocystis PCC6803. 812 90