BIOMAT Database Logo BIOMAT Database Logo

Escherichia coli K-12 copper-containing monoamine oxidase: investigation of the copper binding ligands by site-directed mutagenesis, elemental analysis and topa quinone formation. 1995

J H Roh, and Y Takenaka, and H Suzuki, and K Yamamoto, and H Kumagai
Department of Food Science and Technology, Faculty of Agriculture, Kyoto University, Japan.

Copper-containing monoamine oxidase (EC 1.4.3.6) from Escherichia coli is a periplasmic enzyme containing topa quinone in addition to divalent copper as a cofactor. The amino acid sequence of E. coli monoamine oxidase was compared to several cloned amine oxidase genes and five well-conserved histidine residues were found. Site-directed mutagenesis studies were performed to determine which histidine residue serves as the binding ligand to the copper. Enzyme activity, absorption spectrum, and atomic absorption spectrophotometry of the mutant enzymes indicated that histidines 470, 554, and 556 are the copper binding ligands. The absorption spectra of phenylhydrazine derivatives suggested that copper is necessary for topa quinone formation.

UI MeSH Term Description Entries
D008024 Ligands A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed) Ligand
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008995 Monoamine Oxidase An enzyme that catalyzes the oxidative deamination of naturally occurring monoamines. It is a flavin-containing enzyme that is localized in mitochondrial membranes, whether in nerve terminals, the liver, or other organs. Monoamine oxidase is important in regulating the metabolic degradation of catecholamines and serotonin in neural or target tissues. Hepatic monoamine oxidase has a crucial defensive role in inactivating circulating monoamines or those, such as tyramine, that originate in the gut and are absorbed into the portal circulation. (From Goodman and Gilman's, The Pharmacological Basis of Therapeutics, 8th ed, p415) EC 1.4.3.4. Amine Oxidase (Flavin-Containing),MAO,MAO-A,MAO-B,Monoamine Oxidase A,Monoamine Oxidase B,Type A Monoamine Oxidase,Type B Monoamine Oxidase,Tyramine Oxidase,MAO A,MAO B,Oxidase, Monoamine,Oxidase, Tyramine
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D003300 Copper A heavy metal trace element with the atomic symbol Cu, atomic number 29, and atomic weight 63.55. Copper-63,Copper 63
D004269 DNA, Bacterial Deoxyribonucleic acid that makes up the genetic material of bacteria. Bacterial DNA
D004295 Dihydroxyphenylalanine A beta-hydroxylated derivative of phenylalanine. The D-form of dihydroxyphenylalanine has less physiologic activity than the L-form and is commonly used experimentally to determine whether the pharmacological effects of LEVODOPA are stereospecific. Dopa,3,4-Dihydroxyphenylalanine,3-Hydroxy-DL-tyrosine,Dihydroxyphenylalanine Hydrochloride, (2:1),beta-Hydroxytyrosine,3 Hydroxy DL tyrosine,3,4 Dihydroxyphenylalanine,beta Hydroxytyrosine
D004602 Elements Substances that comprise all matter. Each element is made up of atoms that are identical in number of electrons and protons and in nuclear charge but may differ in mass or number of neutrons. Element
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D006639 Histidine An essential amino acid that is required for the production of HISTAMINE. Histidine, L-isomer,L-Histidine,Histidine, L isomer,L-isomer Histidine

Related Publications

J H Roh, and Y Takenaka, and H Suzuki, and K Yamamoto, and H Kumagai
Cloning and sequencing of a copper-containing, topa quinone-containing monoamine oxidase from human placenta.
November 1996, Gene,
J H Roh, and Y Takenaka, and H Suzuki, and K Yamamoto, and H Kumagai
Spinach carbonic anhydrase: investigation of the zinc-binding ligands by site-directed mutagenesis, elemental analysis, and EXAFS.
November 1994, Biochemistry,
J H Roh, and Y Takenaka, and H Suzuki, and K Yamamoto, and H Kumagai
Mouse coproporphyrinogen oxidase is a copper-containing enzyme: expression in Escherichia coli and site-directed mutagenesis.
January 1996, Biochimica et biophysica acta,
J H Roh, and Y Takenaka, and H Suzuki, and K Yamamoto, and H Kumagai
Site-directed mutagenesis and over expression of aroG gene of Escherichia coli K-12.
December 2012, International journal of biological macromolecules,
J H Roh, and Y Takenaka, and H Suzuki, and K Yamamoto, and H Kumagai
Characterization of a dinucleotide-binding site in monoamine oxidase B by site-directed mutagenesis.
January 1995, Archives of biochemistry and biophysics,
J H Roh, and Y Takenaka, and H Suzuki, and K Yamamoto, and H Kumagai
Investigation of the aurovertin binding site of Escherichia coli F1-ATPase by fluorescence spectroscopy and site-directed mutagenesis.
June 1992, Biochemistry,
J H Roh, and Y Takenaka, and H Suzuki, and K Yamamoto, and H Kumagai
Purification, characterization, and crystallization of monoamine oxidase from Escherichia coli K-12.
September 1994, Bioscience, biotechnology, and biochemistry,
J H Roh, and Y Takenaka, and H Suzuki, and K Yamamoto, and H Kumagai
Copper/topa quinone-containing histamine oxidase from Arthrobacter globiformis. Molecular cloning and sequencing, overproduction of precursor enzyme, and generation of topa quinone cofactor.
March 1995, The Journal of biological chemistry,
J H Roh, and Y Takenaka, and H Suzuki, and K Yamamoto, and H Kumagai
Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis.
May 1989, The Journal of biological chemistry,
J H Roh, and Y Takenaka, and H Suzuki, and K Yamamoto, and H Kumagai
Characterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy.
May 1995, Biochemistry,
Copied contents to your clipboard!