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Literature summary for 1.6.5.5 extracted from

  • Fernandez, M.R.; Porte, S.; Crosas, E.; Barbera, N.; Farres, J.; Biosca, J.A.; Pares, X.
    Human and yeast zeta-crystallins bind AU-rich elements in RNA (2007), Cell. Mol. Life Sci., 64, 1419-1427.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens
expression in Escherichia coli Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0015
-
9,10-phenanthrenequinone pH 7.5 Homo sapiens
0.004
-
9,10-phenanthrenequinone pH 7.5 Saccharomyces cerevisiae
0.005
-
NADPH pH 7.5 Homo sapiens
0.009
-
1,2-naphthoquinone pH 7.5 Saccharomyces cerevisiae
0.029
-
1,2-naphthoquinone pH 7.5 Homo sapiens
0.07
-
NADPH pH 7.5 Saccharomyces cerevisiae

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
14000
-
gel filtration Homo sapiens
36000
-
2 * 36000, SDS-PAGE Saccharomyces cerevisiae
36000
-
4 * 36000, SDS-PAGE Homo sapiens
70000
-
gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens the human and yeast enzymes specifically bind to adenine-uracil rich elements (ARE) in RNA, indicating that both enzymes are ARE-binding proteins and that this property has been conserved in zeta-crystallins throughout evolution. This supports a role for zeta-crystallins as trans-acting factors that could regulate the turnover of certain mRNAs ?
-
?
additional information Saccharomyces cerevisiae the human and yeast enzymes specifically bind to adenine-uracil rich elements (ARE) in RNA, indicating that both enzymes are ARE-binding proteins and that this property has been conserved in zeta-crystallins throughout evolution. This supports a role for zeta-crystallins as trans-acting factors that could regulate the turnover of certain mRNAs ?
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens
-
Saccharomyces cerevisiae

Source Tissue

Source Tissue Comment Organism Textmining
lens
-
Homo sapiens
-
lens
-
Saccharomyces cerevisiae
-

Storage Stability

Storage Stability Organism
4°C, 1 week, complete inactivation of purified enzyme Homo sapiens
4°C, 1 week, complete inactivation of purified enzyme Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,2-naphthoquinone + NADPH + H+ the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal Saccharomyces cerevisiae ? + NADP+
-
?
2 1,2-naphthoquinone + NADPH + H+ the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal Homo sapiens ? + NADP+
-
?
2 9,10-phenanthrenequinone + NADPH + H+ 70% of the activity with 9,10-phenanthrenequinone Homo sapiens ? + NADP+
-
?
9,10-phenanthrenequinone + NADPH + H+ the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal Saccharomyces cerevisiae ? + NADP+
-
?
additional information the human and yeast enzymes specifically bind to adenine-uracil rich elements (ARE) in RNA, indicating that both enzymes are ARE-binding proteins and that this property has been conserved in zeta-crystallins throughout evolution. This supports a role for zeta-crystallins as trans-acting factors that could regulate the turnover of certain mRNAs Homo sapiens ?
-
?
additional information the human and yeast enzymes specifically bind to adenine-uracil rich elements (ARE) in RNA, indicating that both enzymes are ARE-binding proteins and that this property has been conserved in zeta-crystallins throughout evolution. This supports a role for zeta-crystallins as trans-acting factors that could regulate the turnover of certain mRNAs Saccharomyces cerevisiae ?
-
?
additional information enzyme reduces ortho-quinones in the presence of NADPH but is not active with 2-alkenals Homo sapiens ?
-
?
additional information enzyme reduces ortho-quinones in the presence of NADPH but is not active with 2-alkenals Saccharomyces cerevisiae ?
-
?

Subunits

Subunits Comment Organism
homodimer 2 * 36000, SDS-PAGE Saccharomyces cerevisiae
homotetramer 4 * 36000, SDS-PAGE Homo sapiens

Synonyms

Synonyms Comment Organism
zeta-Crystallin
-
Homo sapiens
zeta-Crystallin
-
Saccharomyces cerevisiae
Zta1p
-
Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.2
-
9,10-phenanthrenequinone pH 7.5 Homo sapiens
2.8
-
1,2-naphthoquinone pH 7.5 Homo sapiens
4.17
-
9,10-phenanthrenequinone pH 7.5 Saccharomyces cerevisiae
4.17
-
1,2-naphthoquinone pH 7.5 Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Homo sapiens
7.5
-
assay at Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
NADPH completely specific for NADPH as cofactor Homo sapiens
NADPH completely specific for NADPH as cofactor Saccharomyces cerevisiae