Enzymes
| UniProtKB help_outline | 6 proteins |
Reaction participants Show >> << Hide
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline oxaloacetate Identifier CHEBI:16452 (Beilstein: 3605372; CAS: 149-63-3) help_outline Charge -2 Formula C4H2O5 InChIKeyhelp_outline KHPXUQMNIQBQEV-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 60 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (Beilstein: 1900390; CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 997 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline pyruvate Identifier CHEBI:15361 (Beilstein: 3587721; CAS: 57-60-3) help_outline Charge -1 Formula C3H3O3 InChIKeyhelp_outline LCTONWCANYUPML-UHFFFAOYSA-M SMILEShelp_outline CC(=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 215 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:15641 | RHEA:15642 | RHEA:15643 | RHEA:15644 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Purification and properties of pigeon liver malic enzyme.
RUTTER W.J., LARDY H.A.
J Biol Chem 233:374-382(1958) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Biosynthesis of dicarboxylic acids by carbon dioxide fixation. V. Further study of the "malic" enzyme of Lactobacillus arabinosus.
KAUFMAN S., KORKES S., DEL CAMPILLO A.
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Physiological studies on acid metabolism. 7. Malic enzyme from Kalanchoe crenata: effects of carbon dioxide concentration.
WALKER D.A.
Biochem J 74:216-223(1960) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Some properties of the malic enzyme of pigeon liver. 2. Synthesis of malate from pyruvate.
STICKLAND R.G.
Biochem J 73:654-659(1959) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Some properties of the malic enzyme of pigeon liver. 1. Conversion of malate into pyruvate.
STICKLAND R.G.
Biochem J 73:646-654(1959) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Biosynthesis of dicarboxylic acids by carbon dioxide fixation; isolation and properties of an enzyme from pigeon liver catalyzing the reversible oxidative decarboxylation of 1-malic acid.
OCHOA S., MEHLER A.H., KORNBERG A.
J Biol Chem 174:979-1000(1948) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Biosynthesis of dicarboxylic acids by carbon dioxide fixation. VII. Equilibrium of malic enzyme reaction.
HARARY I., KOREY S.R., OCHOA S.
J Biol Chem 203:595-604(1953) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Studies on regulatory functions of malic enzymes. IV. Effects of sulfhydryl group modification on the catalytic function of NAD-linked malic enzyme from Escherichia coli.
Yamaguchi M.
Reactions catalyzed by NAD-linked malic enzyme from Escherichia coli were investigated. In addition to L-malate oxidative decarboxylase activity (Activity 1) and oxaloacetate decarboxylase activity (Activity 2), the enzyme exhibited oxaloacetate reductase activity (Activity 3) and pyruvate reducta ... >> More
Reactions catalyzed by NAD-linked malic enzyme from Escherichia coli were investigated. In addition to L-malate oxidative decarboxylase activity (Activity 1) and oxaloacetate decarboxylase activity (Activity 2), the enzyme exhibited oxaloacetate reductase activity (Activity 3) and pyruvate reductase activity (Activity 4). Optimum pH's for Activities 3 and 4 were 4.0 and 5.0, and their specific activities were 1.7 and 0.07, respectively. Upon reaction with N-ethylmaleimide (NEM), Activity 1 decreased following pseudo-first order kinetics. Activity 2 decreased in parallel with Activity 1, while Activities 3 and 4 were about ten-fold enhanced by NEM modification. Modification of one or two sulfhydryl groups per enzyme subunit caused an alteration of the activities. Tartronate, a substrate analog, NAD+, and Mn2+ protected the enzyme against the modification. The Km values for the substrates and coenzymes were not significantly affected by NEM modification. Similarly, other sulfhydryl reagents such as p-hydroxymercuribenzoate (PMB), 5,5'-dithiobis(2-nitrobenzoate) (DTNB), and iodoacetate inhibited the decarboxylase activities and activated the reductase activities to various extents. Modification of the enzyme with PMB or DTNB was reversed by the addition of a sulfhydryl compound such as dithiothreitol or 2-mercaptoethanol. Based on the above results, the mechanism of the alteration of enzyme activities by sulfhydryl group modification is discussed. << Less