Literature summary for 1.1.1.40 extracted from

Chang, H.C.; Chen, L.Y.; Lu, Y.H.; Li, M.Y.; Chen, Y.H.; Lin, C.H.; Chang, G.G.
Metal ions stabilize a dimeric molten globule state between the open and closed forms of malic enzyme (2007), Biophys. J., 93, 3977-3988.

Search for more literature for 1.1.1.40

Protein Variants

Protein Variants	Comment	Organism
W252A	site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin	Columba sp.
W252F	site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin	Columba sp.
W252H	site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin	Columba sp.
W252I	site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin	Columba sp.
W252S	site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin	Columba sp.

Inhibitors

Inhibitors	Comment	Organism	Structure
Trypsin	digests the mutant enzymes, while the wild-type enzyme is protected in the presence of Mn2+, because a specific cutting site in the Lys352-Gly-Arg354 region is able to generate a unique polypeptide with Mr of 37 kDa, and this polypeptide is resistant to further digestion	Columba sp.
Urea	inactivation at 3-5 M urea, the pigeon cytosolic NADP+-dependent malic enzyme unfolds and aggregates into various forms with dimers as the basic unit, under the same denaturing conditions but in the presence of 4 mM Mn2+, the enzyme exists exclusively as a molten globule dimer in solution, overview	Columba sp.

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Columba sp.	5829	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mn2+	required for activity and protective against inactivation and degeneration by urea or digestion by trypsin, Trp252 is involved, overview, during the catalytic process of malic enzyme, binding of metal ion induces a conformational change within the enzyme from the open form to an intermediate form, which upon binding of L-malate, transforms further into a catalytically competent closed form	Columba sp.

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
(S)-malate + NADP+	Columba sp.	-	pyruvate + CO2 + NADPH	-	r

Organism

Organism	UniProt	Comment	Textmining
Columba sp.	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(S)-malate + NADP+	-	Columba sp.	pyruvate + CO2 + NADPH	-	r
(S)-malate + NADP+	during the catalytic process of malic enzyme, binding metal ion induces a conformational change within the enzyme from the open form to an intermediate form, which upon binding of L-malate, transforms further into a catalytically competent closed form, overview	Columba sp.	pyruvate + CO2 + NADPH	-	r

Subunits

Subunits	Comment	Organism
More	at 3-5 M urea, the pigeon cytosolic NADP+-dependent malic enzyme unfolds and aggregates into various forms with dimers as the basic unit, under the same denaturing conditions but in the presence of 4 mM Mn2+, the enzyme exists exclusively as a molten globule dimer in solution, aggregation of the enzyme is attributable to the Trp572 side chain, overview	Columba sp.
tetramer	structure analysis from crystal structure, the enzyme is a tetrameric protein with double dimer quaternary structure, pH dependence of enzyme structure, overview	Columba sp.

Synonyms

Synonyms	Comment	Organism
NADP+-dependent malic enzyme	-	Columba sp.

pH Range

pH Minimum	pH Maximum	Comment	Organism
additional information	-	enzyme conformation at different pH values, overview	Columba sp.

Cofactor

Cofactor	Comment	Organism	Structure
NADP+	-	Columba sp.
NADPH	-	Columba sp.

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Release 2023.1 (January 2023)