Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Reaction: 1.8.1.4

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 1.8.1.4

Enzymes and Genes:
dihydrolipoyl dehydrogenase Inferred from experiment : DLD ( Homo sapiens )
lipoamide dehydrogenase Inferred from experiment : DLD ( Gallus gallus )
glycine decarboxylase : AT2G35370 ( Arabidopsis thaliana col )
glycine decarboxylase : AT2G35120 ( Arabidopsis thaliana col )
dihydrolipoamide dehydrogenase : Synpcc7942_1198 ( Synechococcus elongatus PCC 7942 )
dihydrolipoyl dehydrogenase : DLD ( Ascaris suum )
pyruvate dehydrogenase complex E3 component : pdhD ( Synechococcus elongatus PCC 7942 )
dehydrolipoamide dehydrogenase : lpdA ( Advenella mimigardefordensis DPN7 )
lipoamide dehydrogenase Inferred from experiment : lpd ( Escherichia coli K-12 substr. MG1655 )

Sub-reaction of:
glycine + a tetrahydrofolate + NAD+ ↔ a 5,10-methylene-tetrahydrofolate + ammonium + CO2 + NADH

In Pathway: glycine cleavage

Supersedes EC number: 1.6.4.3

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Direct generic reaction:
a [lipoyl-carrier protein] N6-dihydrolipoyl-L-lysine + NAD+ → a [lipoyl-carrier protein] N6-lipoyl-L-lysine + NADH + H+ (1.8.1.4)

Enzyme Commission Primary Name: dihydrolipoyl dehydrogenase

Enzyme Commission Synonyms: LDP-Glc, LDP-Val, dehydrolipoate dehydrogenase, diaphorase, dihydrolipoamide dehydrogenase, dihydrolipoamide:NAD+ oxidoreductase, dihydrolipoic dehydrogenase, dihydrothioctic dehydrogenase, lipoamide dehydrogenase (NADH), lipoamide oxidoreductase (NADH), lipoamide reductase, lipoamide reductase (NADH), lipoate dehydrogenase, lipoic acid dehydrogenase, lipoyl dehydrogenase, protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase

Standard Gibbs Free Energy (ΔrG in kcal/mol): 19.404053 Inferred by computational analysis [Latendresse13]

Summary:
A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [Nesbitt05].

Enzyme Commission Summary:
A flavoprotein (FAD). A component of the multienzyme 2-oxo-acid dehydrogenase complexes. In the pyruvate dehydrogenase complex, it binds to the core of EC 2.3.1.12, dihydrolipoyllysine-residue acetyltransferase, and catalyses oxidation of its dihydrolipoyl groups. It plays a similar role in the oxoglutarate and 3-methyl-2-oxobutanoate dehydrogenase complexes. Another substrate is the dihydrolipoyl group in the H-protein of the glycine-cleavage system (click here for diagram), in which it acts, together with EC 1.4.4.2, glycine dehydrogenase (decarboxylating), and EC 2.1.2.10, aminomethyltransferase, to break down glycine. It can also use free dihydrolipoate, dihydrolipoamide or dihydrolipoyllysine as substrate. This enzyme was first shown to catalyse the oxidation of NADH by methylene blue; this activity was called diaphorase. The glycine cleavage system is composed of four components that only loosely associate: the P protein (EC 1.4.4.2), the T protein (EC 2.1.2.10), the L protein (EC 1.8.1.4) and the lipoyl-bearing H protein [Nesbitt05].

Citations: [Massey60, Savage57, Straub39, Perham00]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.8.1.4 , ENZYME:EC:1.8.1.4 , IUBMB-ExplorEnz:EC:1.8.1.4

Credits:
Revised 18-Sep-2012 by Caspi R , SRI International


References

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Massey60: Massey V, Gibson QH, Veeger C (1960). "Intermediates in the catalytic action of lipoyl dehydrogenase (diaphorase)." Biochem J 77;341-51. PMID: 13767908

Nesbitt05: Nesbitt NM, Baleanu-Gogonea C, Cicchillo RM, Goodson K, Iwig DF, Broadwater JA, Haas JA, Fox BG, Booker SJ (2005). "Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase." Protein Expr Purif 39(2);269-82. PMID: 15642479

Perham00: Perham RN (2000). "Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions." Annu Rev Biochem 69;961-1004. PMID: 10966480

Savage57: Savage N (1957). "Preparation and properties of highly purified diaphorase." Biochem J 67(1);146-55. PMID: 13471525

Straub39: Straub FB (1939). "Isolation and properties of a flavoprotein from heart muscle tissue." Biochem J 33(5);787-92. PMID: 16746974


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, biocyc13.