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Literature summary extracted from

  • Collins, R.; Johansson, A.L.; Karlberg, T.; Markova, N.; van den Berg, S.; Olesen, K.; Hammarstroem, M.; Flores, A.; Schueler, H.; Schiavone, L.H.; Brzezinski, P.; Arner, E.S.; Hoegbom, M.
    Biochemical discrimination between selenium and sulfur 1: a single residue provides selenium specificity to human selenocysteine lyase (2012), PLoS ONE, 7, e30581.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.4.1.16 sequence comparisons, recombinant expression of N-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.4.1.16 purified enzyme in dimeric and tetrameric forms, sitting drop vapour diffusion method, 100 nl of 17 mg/ml protein solution with 100 nl of well solution 1 containing 100 mM HEPES, pH 6.7, and 10% PEG 6000, or well solution 2 containing 50 mM HEPES, pH 8.1, 200 mM ammonium nitrate and 25% PEG 3350, 20°C, 3 days or 7 days, respectively, X-ray diffraction structure determination and analysis of the two crystals forms at 2.1 A and 1.8 A resolution, respectively, modeling of dimeric enzyme complexed with pyridoxal 5'-phosphate Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
4.4.1.16 D146K site-directed mutagenesis, the mutant variant shows loss of selenocysteine specificity and appearance of cysteine desulfurase activity Homo sapiens
4.4.1.16 D146K/H389T site-directed mutagenesis,the mutant variant shows loss of selenocysteine specificity and appearance of cysteine desulfurase activity to a higher extent Homo sapiens
4.4.1.16 H389T site-directed mutagenesis, the mutant variant shows loss of selenocysteine specificity and appearance of cysteine desulfurase activity Homo sapiens
4.4.1.16 V256S site-directed mutagenesis, the mutant variant shows loss of selenocysteine specificity and appearance of cysteine desulfurase activity Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.4.1.16 L-selenocysteine + reduced acceptor Homo sapiens
-
 selenide + L-alanine + acceptor
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.16 Homo sapiens Q96I15
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.4.1.16 recombinant N-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration, followed by tag cleavage through TEV protease, another step of nickel affinity chromatography, and dialysis Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.16 L-selenocysteine + reduced acceptor
-
 Homo sapiens selenide + L-alanine + acceptor
-
 ?
4.4.1.16 additional information the enzyme is specific for L-selenocysteine versus L-cysteine, substrate specificity for selenium and sulfur is determined by a single residue, Asp246, in human selenocysteine lyase Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.4.1.16 SCL
-
 Homo sapiens
4.4.1.16 Sec lyase
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.4.1.16 37
-
 assay at Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.4.1.16 80
-
 purified enzyme, pH 8.5, 2 min, inactivation Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.4.1.16 8.5
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
4.4.1.16 pyridoxal 5'-phosphate
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
4.4.1.16 additional information the enzyme adopts the canonical fold type I structure of pyridoxal 5'-phosphate enzymes with an active site cysteine, C388 Homo sapiens