Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-10-12
pubmed:abstractText
Catalase is a ubiquitous enzyme present in both the prokaryotic and eukaryotic cells of aerobic organisms. It serves, in part, to protect the cell from the toxic effects of small peroxides. Escherichia coli produces two catalases, HPI and HPII, that are quite distinct from other catalases in physical structure and catalytic properties. HPII, studied in this work, is encoded by the katE gene, and has been characterized as an oligomeric, monofunctional catalase containing one cis-heme d prosthetic group per subunit of 753 residues.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
491-502
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7663946-Amino Acid Sequence, pubmed-meshheading:7663946-Animals, pubmed-meshheading:7663946-Bacterial Proteins, pubmed-meshheading:7663946-Binding Sites, pubmed-meshheading:7663946-Catalase, pubmed-meshheading:7663946-Cattle, pubmed-meshheading:7663946-Crystallography, X-Ray, pubmed-meshheading:7663946-Escherichia coli, pubmed-meshheading:7663946-Fungal Proteins, pubmed-meshheading:7663946-Heme, pubmed-meshheading:7663946-Hydrogen Bonding, pubmed-meshheading:7663946-Liver, pubmed-meshheading:7663946-Micrococcus, pubmed-meshheading:7663946-Models, Molecular, pubmed-meshheading:7663946-Molecular Sequence Data, pubmed-meshheading:7663946-Penicillium, pubmed-meshheading:7663946-Protein Conformation, pubmed-meshheading:7663946-Proteus mirabilis, pubmed-meshheading:7663946-Sequence Alignment, pubmed-meshheading:7663946-Sequence Homology, Amino Acid, pubmed-meshheading:7663946-Structure-Activity Relationship
pubmed:year
1995
pubmed:articleTitle
Crystal structure of catalase HPII from Escherichia coli.
pubmed:affiliation
Departamento de Ingeniería Química, Universidad Politécnica de Catalunña, Barcelona, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't