Methionine aminopeptidase associated with liver mitochondria and microsomes

Freitas, J.O.; Termignoni, Carlos; Borges, Durval Rosa; Sampaio, Cláudio Hoffmann; Prado, J. L.; Guimarães, Jorge A.

doi:10.1016/0020-711x(81)90004-5

Cited by 12 publications

(7 citation statements)

References 19 publications

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“…This indicates an efficient blockage of the Nterminal processing of Met by TFM. In many cases, this initiator Met is cotranslationally removed by a Met-aminopeptidase [28]. It is well-known that Met metabolism plays a role in many aspects of cellular physiology.…”

mentioning

confidence: 99%

Efforts towards the Design of ‘Teflon’ Proteins: In vivo Translation with Trifluorinated Leucine and Methionine Analogues

Budiša

Pipitone

Siwanowicz

et al. 2004

Chemistry & Biodiversity

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In vivo incorporation of monofluorinated noncanonical amino acids into recombinant proteins has been well-established for decades. Proteins fluorinated in this way proved to be useful tools for many practical applications. In contrast, trifluorinated amino acids have been incorporated in only a few peptides and relatively small proteins by using expression systems in living cells. A novel class of proteins with a fluorous core can be envisaged only if full replacement of the core-building hydrophobic and aliphatic amino acids such as leucine or methionine with the related analogues trifluoromethionine and trifluoroleucine would be feasible. However, our systematic efforts to introduce these amino acids in larger proteins (over 10 Da) that contain different structural motifs clearly show that only partial substitutions are possible. The reasons are high toxicity of these substances and difficulties to accommodate them into the compact cores of natural proteins without adverse effects on their structural integrity. Therefore, engineering of such three dimensional 'Teflon'-like structures would require, besides an expansion of the amino acid repertoire of the genetic code, a de novo protein design as well.

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mentioning

confidence: 99%

Efforts towards the Design of ‘Teflon’ Proteins: In vivo Translation with Trifluorinated Leucine and Methionine Analogues

Budiša

Pipitone

Siwanowicz

et al. 2004

Chemistry & Biodiversity

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“…Thus clear evidence for the presence of such an enzyme and of its characterization have not been provided so far, although its existence is widely accepted. We have previously shown that rat liver subcellular fractions contain a typical methionine aminopeptidase distinct from previously described arylaminopeptidases (Freitas et al, 1981(Freitas et al, , 1985. In the present work we have further studied the properties of this aminopeptidase, with special reference to its ability to hydrolyse substrates containing N-terminal methionine in amino acid derivatives as well as peptides, including haemoglobin nascent peptides.…”

Section: Introductionmentioning

confidence: 72%

“…However, at least four distinct arylamidase activities could be separated after detergent solubilization and DEAE-cellulose chromatography (Freitas et al, 1981). It is now shown that two of these enzymes are active on splitting methionine 2-naphthylamide ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Rat liver homogenate contains several enzymes displaying arylamidase activity, the highest activity always being that towards methionine 2-naphthylamide (Makinen & Raekallio, 1968;Freitas et al, 1981).…”

Section: Resultsmentioning

confidence: 99%

“…The integrity of the particles was checked and confirmed by electron microscopy as well as by using the enzyme markers glutamate dehydrogenase, glucose-6-phosphatase and tartrate-inhibitable acid phosphatase. Enzyme fractionation MAP was prepared as described previously (Freitas et al, 1981). Rat liver homogenate or its subcellular organelles were treated with Triton X-100 in a detergent/protein ratio of 5: 1 (w/w).…”

Section: Subcellular Fractionsmentioning

confidence: 99%

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