Protein phylogenetically related

Comparisons of amino acid sequences have revealed that some type 2 copper proteins are phylogenetically related to non-copper proteins of similar func-... 

Galactose oxidase has a unique tertiary structure for a copper protein, comparable with that of the non-copper protein methylamine dehydrogenase. Comparisons of the amino acid sequences [157] show, however, that the enzymes are not phylogenetically related. The tertiary structures developed separately [30]. 

Two phenylalanine hydroxylases have been described, one containing iron and one containing copper. Both are phylogenetically related to the group of enzymes which hydroxylate aromatic amino acids, including tryptophane and tyrosine hydroxylase [187]. No phylogenetic relationship could be constructed to other proteins [183-186,327]. 

All copper proteins which are known to be phylogenetically related to noncopper proteins - i. e., the small blue proteins, metallothioneins and some type 2 copper proteins - are found in single-celled organisms. Hemocyanins, blue oxidases, and those type 2 copper proteins whose functions are essential for multicellular life-forms are not phylogenetically related to non-copper proteins and do not occur in single-celled organisms. 

Balz, M. L. et al. 1982. Phylogenetic aspects of C-reactive protein and related proteins. Annals of the New York Academy of Sciences 389 49-73. 

Ceruloplasmin a blue, copper-containing glycoprotein, which is present in mammalian blo plasma, and which is phylogenetically related to plant lac-cases and to ascorbate oxidase, both of which are blue. It is a transport and/or storage protein for copper, and it is also an oxidase. Substrates include unsaturated compounds, such as indole derivatives, amphetamine, adrenalin and dopamine. C. has a central role in copper metabolism when C. is absent, as in Wilson s disease, copper is deposited in the tissues, causing death. 

The primary and even tertiary structure of M. and hemoglobins from many different species show striking similarities. M. appears to be phylogenetically the oldest known heme protein, from which hemoglobin evolved as an independent molecule 600 million years ago. M. also appears to be phylogenetically related to Leghemoglobin (see). 

Histone Deacetylases (HDACs) catalyze the removal of the acetyl groups from lysines (see Fig. 1). Together with the HATs they are responsible for maintaining the level of histone acetylation throughout the genome. The family of HDAC proteins has been divided into four classes based on phylogenetic analysis and sequence comparison. HDACs of the classes I and II share the same Zn2+-based reaction and are evolutionary related. Class IV HDACs also possess a Zn2+-based reaction... 

Figure 1 shows the phylogenetic relationship of the mitochondrial and bacterial Rieske proteins. Plant mitochondrial Rieske proteins form a separate cluster, whereas bacterial Rieske proteins are more closely related to Rieske proteins from fungi or mammals, although the subunit composition and organization of the bci complex is compa-... 

Now described as a trp superfamily, more than 20 vertebrate trp homologs have been identified and these can be divided phylogenetically into three subfamilies trpC (termed canonical as they are most closely related to Drosophila trp), trpV and trpM. Some of these proteins are potential contenders for the capacitative calcium ion entry channel. In particular, expression of members of the TRPC and TRPV families in mammalian cells has been shown to augment capacitative calcium ion entry, but their role is still a matter for debate [17]. 

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