Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.5.5 0.0015
-
 9,10-phenanthrenequinone pH 7.5 Homo sapiens
1.6.5.5 0.004
-
 9,10-phenanthrenequinone pH 7.5 Saccharomyces cerevisiae
1.6.5.5 0.005
-
 NADPH pH 7.5 Homo sapiens
1.6.5.5 0.009
-
 1,2-naphthoquinone pH 7.5 Saccharomyces cerevisiae
1.6.5.5 0.029
-
 1,2-naphthoquinone pH 7.5 Homo sapiens
1.6.5.5 0.07
-
 NADPH pH 7.5 Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.6.5.5 14000
-
 gel filtration Homo sapiens
1.6.5.5 36000
-
 2 * 36000, SDS-PAGE Saccharomyces cerevisiae
1.6.5.5 36000
-
 4 * 36000, SDS-PAGE Homo sapiens
1.6.5.5 70000
-
 gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.5.5 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 ?
-
 ?
1.6.5.5 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

EC Number Organism UniProt Comment Textmining
1.6.5.5 Homo sapiens
-
-
-
1.6.5.5 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.5.5
-
 Homo sapiens
1.6.5.5
-
 Saccharomyces cerevisiae

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.6.5.5 lens
-
 Homo sapiens
-
1.6.5.5 lens
-
 Saccharomyces cerevisiae
-

Storage Stability

EC Number Storage Stability Organism
1.6.5.5 4°C, 1 week, complete inactivation of purified enzyme Homo sapiens
1.6.5.5 4°C, 1 week, complete inactivation of purified enzyme Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.5.5 1,2-naphthoquinone + NADPH + H+ the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal Saccharomyces cerevisiae ? + NADP+
-
 ?
1.6.5.5 2 1,2-naphthoquinone + NADPH + H+ the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal Homo sapiens ? + NADP+
-
 ?
1.6.5.5 2 9,10-phenanthrenequinone + NADPH + H+ 70% of the activity with 9,10-phenanthrenequinone Homo sapiens ? + NADP+
-
 ?
1.6.5.5 9,10-phenanthrenequinone + NADPH + H+ the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal Saccharomyces cerevisiae ? + NADP+
-
 ?
1.6.5.5 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 ?
-
 ?
1.6.5.5 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 ?
-
 ?
1.6.5.5 additional information enzyme reduces ortho-quinones in the presence of NADPH but is not active with 2-alkenals Homo sapiens ?
-
 ?
1.6.5.5 additional information enzyme reduces ortho-quinones in the presence of NADPH but is not active with 2-alkenals Saccharomyces cerevisiae ?
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.6.5.5 zeta-Crystallin
-
 Homo sapiens
1.6.5.5 zeta-Crystallin
-
 Saccharomyces cerevisiae
1.6.5.5 Zta1p
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6.5.5 2.2
-
 9,10-phenanthrenequinone pH 7.5 Homo sapiens
1.6.5.5 2.8
-
 1,2-naphthoquinone pH 7.5 Homo sapiens
1.6.5.5 4.17
-
 9,10-phenanthrenequinone pH 7.5 Saccharomyces cerevisiae
1.6.5.5 4.17
-
 1,2-naphthoquinone pH 7.5 Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.6.5.5 7.5
-
 assay at Homo sapiens
1.6.5.5 7.5
-
 assay at Saccharomyces cerevisiae

Cofactor

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