M00163
type: Enzyme
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/-.-.-.-
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/3.-.-.-
cath: http://ezcatdb.cbrc.jp/EzCatDB/cath/2.-.-.-
cath: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
cath: FAD/NAD(P)-binding domain
cath: Enolase-like; domain 1
ec: https://purl.uniprot.org/enzyme/1.4.4.2
ec: https://purl.uniprot.org/enzyme/2.1.2.10
ec: https://purl.uniprot.org/enzyme/1.8.1.4
uniprot: P49095
uniprot: P26969
uniprot: P23378
uniprot: P48015
uniprot: P49364
uniprot: P48728
uniprot: P39726
uniprot: P16048
uniprot: P23434
uniprot: P09624
uniprot: P31023
uniprot: P09622
kegg enzyme: glycine dehydrogenase (decarboxylating)
  type: KeggEnzyme
  ec: https://purl.uniprot.org/enzyme/1.4.4.2
kegg pathway: Glycolysis / Gluconeogenesis
kegg pathway: Citrate cycle (TCA cycle)
kegg pathway: Glycine, serine and threonine metabolism
kegg pathway: Valine, leucine and isoleucine degradation
kegg pathway: Pyruvate metabolism
kegg pathway: One carbon pool by folate
kegg pathway: Nitrogen metabolism
kegg cofactor: Pyridoxal phosphate
kegg cofactor: FAD
kegg substrate: Glycine
kegg substrate: Lipoylprotein
kegg substrate: S-Aminomethyldihydrolipoylprotein
kegg substrate: Tetrahydrofolate
kegg substrate: Dihydrolipoylprotein
kegg substrate: NAD+
kegg product: S-Aminomethyldihydrolipoylprotein
kegg product: CO2
kegg product: Dihydrolipoylprotein
kegg product: 5,10-methylenetetrahydrofolate
kegg product: NH3
kegg product: Lipoylprotein
kegg product: NADH
kegg product: H+
pdb: 1wsrA01
pdb: 1wsrB01
pdb: 1wsvA01
pdb: 1wsvB01
pdb: 1wsrA02
pdb: 1wsrB02
pdb: 1wsvA02
pdb: 1wsvB02
pdb: 1dxmA
pdb: 1dxmB
pdb: 1hpcA
pdb: 1hpcB
pdb: 1htpA
pdb: 1jehA01
pdb: 1jehB01
pdb: 1v59A01
pdb: 1v59B01
pdb: 1dxlA01
pdb: 1dxlB01
pdb: 1dxlC01
pdb: 1dxlD01
pdb: 1zmcA01
pdb: 1zmcB01
pdb: 1zmcC01
pdb: 1zmcD01
pdb: 1zmcE01
pdb: 1zmcF01
pdb: 1zmcG01
pdb: 1zmcH01
pdb: 1zmdA01
pdb: 1zmdB01
pdb: 1zmdC01
pdb: 1zmdD01
pdb: 1zmdE01

OB fold (Dihydrolipoamide Acetyltransferase, E2P)
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/2.40.50.100

FAD/NAD(P)-binding domain
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.50.50.60
catalytic domain: index.html

Enolase-like; domain 1
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.30.390.30
catalytic domain: index.html

Glycolysis / Gluconeogenesis
type: KeggPathway
references: KEGG:MAP00010
ec: https://purl.uniprot.org/enzyme/1.8.1.4

Citrate cycle (TCA cycle)
type: KeggPathway
references: KEGG:MAP00020
ec: https://purl.uniprot.org/enzyme/1.8.1.4

Glycine, serine and threonine metabolism
type: KeggPathway
references: KEGG:MAP00260
ec: https://purl.uniprot.org/enzyme/1.4.4.2
ec: https://purl.uniprot.org/enzyme/2.1.2.10
ec: https://purl.uniprot.org/enzyme/1.8.1.4

Valine, leucine and isoleucine degradation
type: KeggPathway
references: KEGG:MAP00280
ec: https://purl.uniprot.org/enzyme/1.8.1.4

Pyruvate metabolism
type: KeggPathway
references: KEGG:MAP00620
ec: https://purl.uniprot.org/enzyme/1.8.1.4

One carbon pool by folate
type: KeggPathway
references: KEGG:MAP00670
ec: https://purl.uniprot.org/enzyme/2.1.2.10

Nitrogen metabolism
type: KeggPathway
references: KEGG:MAP00910
ec: https://purl.uniprot.org/enzyme/2.1.2.10

Pyridoxal phosphate
type: KeggCofactor
references: KEGG:C00018
references: CHEBI:18405
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/1.4.4.2
compound type: aromatic ring (with nitrogen atoms)
compound type: phosphate group/phosphate ion

FAD
type: KeggCofactor
references: KEGG:C00016
references: CHEBI:16238
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/1.8.1.4
compound type: amide group
compound type: amine group
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
compound type: carbohydrate
compound type: nucleotide

Glycine
type: KeggSubstrate
references: KEGG:C00037
references: CHEBI:15428
references: CHEBI:57305
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/1.4.4.2
compound type: amino acids

Lipoylprotein
type: KeggSubstrate
type: KeggProduct
references: KEGG:C02051
ec: https://purl.uniprot.org/enzyme/1.4.4.2
ec: https://purl.uniprot.org/enzyme/1.8.1.4
compound type: disulfide bond
compound type: lipid
compound type: peptide/protein

S-Aminomethyldihydrolipoylprotein
type: KeggSubstrate
type: KeggProduct
references: KEGG:C01242
ec: https://purl.uniprot.org/enzyme/2.1.2.10
ec: https://purl.uniprot.org/enzyme/1.4.4.2
compound type: amine group
compound type: lipid
compound type: peptide/protein
compound type: sulfhydryl group
compound type: sulfide group

Tetrahydrofolate
type: KeggSubstrate
references: KEGG:C00101
references: CHEBI:15635
references: CHEBI:20506
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/2.1.2.10
compound type: amino acids
compound type: amide group
compound type: amine group
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
compound type: carboxyl group

Dihydrolipoylprotein
type: KeggSubstrate
type: KeggProduct
references: KEGG:C02972
ec: https://purl.uniprot.org/enzyme/1.8.1.4
ec: https://purl.uniprot.org/enzyme/2.1.2.10
compound type: carbohydrate
compound type: lipid
compound type: peptide/protein
compound type: sulfhydryl group

NAD+
type: KeggSubstrate
references: KEGG:C00003
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/1.8.1.4
compound type: amide group
compound type: amine group
compound type: nucleotide

CO2
type: KeggProduct
references: KEGG:C00011
references: CHEBI:16526
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/1.4.4.2
compound type: others

5,10-methylenetetrahydrofolate
type: KeggProduct
references: KEGG:C00143
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/2.1.2.10
compound type: amino acids
compound type: amide group
compound type: amine group
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
compound type: carboxyl group

NH3
type: KeggProduct
references: KEGG:C00014
references: CHEBI:16134
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/2.1.2.10
compound type: amine group
compound type: organic ion

NADH
type: KeggProduct
references: KEGG:C00004
references: CHEBI:16908
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/1.8.1.4
compound type: amide group
compound type: amine group
compound type: nucleotide

H+
type: KeggProduct
references: KEGG:C00080
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi
ec: https://purl.uniprot.org/enzyme/1.8.1.4
compound type: others

1wsrA01
type: Pdb
references: 1wsr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wsr
catalytic residue: ASP 101

1wsrB01
type: Pdb
references: 1wsr
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wsr
catalytic residue: ASP 101

1wsvA01
type: Pdb
references: 1wsv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wsv
catalytic residue: ASP 101

1wsvB01
type: Pdb
references: 1wsv
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1wsv
catalytic residue: ASP 101

1dxmA
type: Pdb
references: 1dxm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxm
cofactor binding residue: LYS 63(lipoyl cofactor binding)

1dxmB
type: Pdb
references: 1dxm
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxm
cofactor binding residue: LYS 63(lipoyl cofactor binding)

1hpcA
type: Pdb
references: 1hpc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpc
cofactor binding residue: LYS 63(lipoyl cofactor binding)

1hpcB
type: Pdb
references: 1hpc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1hpc
cofactor binding residue: LYS 63(lipoyl cofactor binding)

1htpA
type: Pdb
references: 1htp
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1htp
cofactor binding residue: LYS 63(lipoyl cofactor binding)

1jehA01
type: Pdb
references: 1jeh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jeh
catalytic residue: TYR 18;CYS 44;CYS 49

1jehB01
type: Pdb
references: 1jeh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jeh
catalytic residue: TYR 18;CYS 44;CYS 49

1v59A01
type: Pdb
references: 1v59
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v59
catalytic residue: TYR 18;CYS 44;CYS 49

1v59B01
type: Pdb
references: 1v59
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v59
catalytic residue: TYR 18;CYS 44;CYS 49

1dxlA01
type: Pdb
references: 1dxl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxl
catalytic residue: TYR 19;CYS 45;CYS 50

1dxlB01
type: Pdb
references: 1dxl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxl
catalytic residue: TYR 19;CYS 45;CYS 50

1dxlC01
type: Pdb
references: 1dxl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxl
catalytic residue: TYR 19;CYS 45;CYS 50

1dxlD01
type: Pdb
references: 1dxl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxl
catalytic residue: TYR 19;CYS 45;CYS 50

1zmcA01
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: TYR 19;CYS 45;CYS 50

1zmcB01
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: TYR 19;CYS 45;CYS 50

1zmcC01
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: TYR 19;CYS 45;CYS 50

1zmcD01
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: TYR 19;CYS 45;CYS 50

1zmcE01
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: TYR 19;CYS 45;CYS 50

1zmcF01
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: TYR 19;CYS 45;CYS 50

1zmcG01
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: TYR 19;CYS 45;CYS 50

1zmcH01
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: TYR 19;CYS 45;CYS 50

1zmdA01
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: TYR 19;CYS 45;CYS 50

1zmdB01
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: TYR 19;CYS 45;CYS 50

1zmdC01
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: TYR 19;CYS 45;CYS 50

1zmdD01
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: TYR 19;CYS 45;CYS 50

1zmdE01
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: TYR 19;CYS 45;CYS 50

1zmdF01
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: TYR 19;CYS 45;CYS 50

1zmdG01
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: TYR 19;CYS 45;CYS 50

1zmdH01
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: TYR 19;CYS 45;CYS 50

1jehA03
type: Pdb
references: 1jeh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jeh
catalytic residue: HIS 457;HIS 477

1jehB03
type: Pdb
references: 1jeh
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1jeh
catalytic residue: HIS 457;HIS 477

1v59A03
type: Pdb
references: 1v59
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v59
catalytic residue: HIS 457;HIS 477

1v59B03
type: Pdb
references: 1v59
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1v59
catalytic residue: HIS 457;HIS 477

1dxlA03
type: Pdb
references: 1dxl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxl
catalytic residue: HIS 449;HIS 469

1dxlB03
type: Pdb
references: 1dxl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxl
catalytic residue: HIS 449;HIS 469

1dxlC03
type: Pdb
references: 1dxl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxl
catalytic residue: HIS 449;HIS 469

1dxlD03
type: Pdb
references: 1dxl
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxl
catalytic residue: HIS 449;HIS 469

1zmcA03
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: HIS 452;ASN 473

1zmcB03
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: HIS 452;ASN 473

1zmcC03
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: HIS 452;ASN 473

1zmcD03
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: HIS 452;ASN 473

1zmcE03
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: HIS 452;ASN 473

1zmcF03
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: HIS 452;ASN 473

1zmcG03
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: HIS 452;ASN 473

1zmcH03
type: Pdb
references: 1zmc
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmc
catalytic residue: HIS 452;ASN 473

1zmdA03
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: HIS 452;ASN 473

1zmdB03
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: HIS 452;ASN 473

1zmdC03
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: HIS 452;ASN 473

1zmdD03
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: HIS 452;ASN 473

1zmdE03
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: HIS 452;ASN 473

1zmdF03
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: HIS 452;ASN 473

1zmdG03
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: HIS 452;ASN 473

1zmdH03
type: Pdb
references: 1zmd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1zmd
catalytic residue: HIS 452;ASN 473

Analogue
compound: Tetrahydrofolate
pdb: 1wsvA01
ligand het code: THH

Analogue
compound: Tetrahydrofolate
pdb: 1wsvB01
ligand het code: THH

Analogue
compound: NAD+
pdb: 1v59A02
ligand het code: NAD

Analogue
compound: NAD+
pdb: 1v59B02
ligand het code: NAD

Analogue
compound: NAD+
pdb: 1zmcB02
ligand het code: NAD

Analogue
compound: NAD+
pdb: 1zmcC02
ligand het code: NAD

Analogue
compound: NAD+
pdb: 1zmcE02
ligand het code: NAD

Analogue
compound: NAD+
pdb: 1zmcF02
ligand het code: NAD

Analogue
compound: NAD+
pdb: 1zmcG02
ligand het code: NAD

Analogue
compound: NAD+
pdb: 1zmcH02
ligand het code: NAD

ReferenceForCatalyticMechanism
reference index: 20
reference section: Fig.3, p.1148-1151

The mitochondrial glycine cleavage system. Unique features of the glycine decarboxylation.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/6750353
journal: Mol Cell Biochem
volume: 45
pages: 137-49
published year: 1982
authors:
  item: Kikuchi G
  item: Hiraga K

Crystallographic data for H-protein from the glycine decarboxylase complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1856858
journal: J Mol Biol
volume: 220
pages: 223-4
published year: 1991
authors:
  item: Sieker L
  item: Cohen-Addad C
  item: Neuburger M
  item: Douce R

X-ray structure determination at 2.6-A resolution of a lipoate-containing protein: the H-protein of the glycine decarboxylase complex from pea leaves.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS)
medline id: 94255425
references: http://www.ncbi.nlm.nih.gov/pubmed/8197146
references: P16048
journal: Proc Natl Acad Sci U S A
volume: 91
pages: 4850-3
published year: 1994
authors:
  item: Pares S
  item: Cohen-Addad C
  item: Sieker L
  item: Neuburger M
  item: Douce R

Refined structures at 2 and 2.2 A resolution of two forms of the H-protein, a lipoamide-containing protein of the glycine decarboxylase complex.
type: BibliographicResource
comment: X-ray crystallography
journal: Acta Crystallogr D Biol Crystallogr
volume: 51
pages: 1041-51
published year: 1995
authors:
  item: Pares S
  item: Cohenaddad C
  item: Sieker LC
  item: Neuburger M
  item: Douce R
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

The lipoamide arm in the glycine decarboxylase complex is not freely swinging.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/7719855
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Nat Struct Biol
volume: 2
pages: 63-8
published year: 1995
authors:
  item: Cohen-Addad C
  item: Pares S
  item: Sieker L
  item: Neuburger M
  item: Douce R

Specific induction by glycine of the gene for the P-subunit of glycine decarboxylase from Saccharomyces cerevisiae.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8830251
journal: Mol Microbiol
volume: 19
pages: 611-23
published year: 1996
authors:
  item: Sinclair DA
  item: Hong SP
  item: Dawes IW

Structural studies of the glycine decarboxylase complex from pea leaf mitochondria.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9479445
journal: Biochimie
volume: 79
pages: 637-43
published year: 1997
authors:
  item: Cohen-Addad C
  item: Faure M
  item: Neuburger M
  item: Ober R
  item: Sieker L
  item: Bourguignon J
  item: Macherel D
  item: Douce R

Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9538259
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Biochem (Tokyo)
volume: 123
pages: 668-74
published year: 1998
authors:
  item: Toyoda T
  item: Suzuki K
  item: Sekiguchi T
  item: Reed LJ
  item: Takenaka A

Investigation of the local structure and dynamics of the H subunit of the mitochondrial glycine decarboxylase using heteronuclear NMR spectroscopy.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10387079
journal: Biochemistry
volume: 38
pages: 8334-46
published year: 1999
authors:
  item: Guilhaudis L
  item: Simorre JP
  item: Blackledge M
  item: Neuburger M
  item: Bourguignon J
  item: Douce R
  item: Marion D
  item: Gans P

Biochemical dissection of photorespiration.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10375564
journal: Curr Opin Plant Biol
volume: 2
pages: 214-22
published year: 1999
authors:
  item: Douce R
  item: Neuburger M

Structural and functional characterization of H protein mutants of the glycine decarboxylase complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10473591
journal: J Biol Chem
volume: 274
pages: 26344-52
published year: 1999
authors:
  item: Gueguen V
  item: Macherel D
  item: Neuburger M
  item: Pierre CS
  item: Jaquinod M
  item: Gans P
  item: Douce R
  item: Bourguignon J

Backbone and sequence-specific assignment of three forms of the lipoate-containing H-protein of the glycine decarboxylase complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10605092
journal: J Biomol NMR
volume: 15
pages: 185-6
published year: 1999
authors:
  item: Guilhaudis L
  item: Simorre JP
  item: Bouchayer E
  item: Neuburger M
  item: Bourguignon J
  item: Douce R
  item: Marion D
  item: Gans P

Theoretical study of the conformation of the H-protein lipoamide arm as a function of its terminal group.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10398369
journal: Proteins
volume: 36
pages: 228-37
published year: 1999
authors:
  item: Roche O
  item: Hinsen K
  item: Field MJ

Combined structural and biochemical analysis of the H-T complex in the glycine decarboxylase cycle: evidence for a destabilization mechanism of the H-protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10757974
journal: Biochemistry
volume: 39
pages: 4259-66
published year: 2000
authors:
  item: Guilhaudis L
  item: Simorre JP
  item: Blackledge M
  item: Marion D
  item: Gans P
  item: Neuburger M
  item: Douce R

Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10806386
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: Eur J Biochem
volume: 267
pages: 2890-8
published year: 2000
authors:
  item: Faure M
  item: Bourguignon J
  item: Neuburger M
  item: MacHerel D
  item: Sieker L
  item: Ober R
  item: Kahn R
  item: Cohen-Addad C
  item: Douce R

Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 1. Biochemical studies.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10806385
journal: Eur J Biochem
volume: 267
pages: 2882-9
published year: 2000
authors:
  item: Neuburger M
  item: Polidori AM
  item: Pietre E
  item: Faure M
  item: Jourdain A
  item: Bourguignon J
  item: Pucci B
  item: Douce R

Theoretical study of the conformation of the lipoamide arm in a mutant H protein.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11599027
journal: Proteins
volume: 45
pages: 237-40
published year: 2001
authors:
  item: Roche O
  item: Field MJ

The glycine decarboxylase system: a fascinating complex.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11286922
journal: Trends Plant Sci
volume: 6
pages: 167-76
published year: 2001
authors:
  item: Douce R
  item: Bourguignon J
  item: Neuburger M
  item: Rebeille F

Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15946682
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Mol Biol
volume: 350
pages: 543-52
published year: 2005
authors:
  item: Brautigam CA
  item: Chuang JL
  item: Tomchick DR
  item: Machius M
  item: Chuang DT

Crystal structure of human T-protein of glycine cleavage system at 2.0 A resolution and its implication for understanding non-ketotic hyperglycinemia.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/16051266
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
journal: J Mol Biol
volume: 351
pages: 1146-59
published year: 2005
authors:
  item: Okamura-Ikeda K
  item: Hosaka H
  item: Yoshimura M
  item: Yamashita E
  item: Toma S
  item: Nakagawa A
  item: Fujiwara K
  item: Motokawa Y
  item: Taniguchi H

P-protein
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.4.4.2

glycine decarboxylase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.4.4.2

glycine-cleavage complex
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.4.4.2

glycine:lipoylprotein oxidoreductase (decarboxylating andacceptor-aminomethylating)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.4.4.2

protein P1
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.4.4.2

aminomethyltransferase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.1.2.10

S-aminomethyldihydrolipoylprotein:(6S)-tetrahydrofolateaminomethyltransferase (ammonia-forming)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.1.2.10

T-protein
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.1.2.10

glycine synthase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.1.2.10

tetrahydrofolate aminomethyltransferase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.1.2.10

[protein]-8-S-aminomethyldihydrolipoyllysine:tetrahydrofolateaminomethyltransferase (ammonia-forming)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/2.1.2.10

dihydrolipoyl dehydrogenase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

LDP-Glc
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

LDP-Val
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

dehydrolipoate dehydrogenase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

diaphorase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

dihydrolipoamide dehydrogenase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

dihydrolipoamide:NAD+ oxidoreductase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

dihydrolipoic dehydrogenase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

dihydrothioctic dehydrogenase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

lipoamide dehydrogenase (NADH)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

lipoamide oxidoreductase (NADH)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

lipoamide reductase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

lipoamide reductase (NADH)
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

lipoate dehydrogenase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

lipoic acid dehydrogenase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

lipoyl dehydrogenase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4

protein-6-N-(dihydrolipoyl)lysine:NAD+ oxidoreductase
type: KeggEnzyme
ec: https://purl.uniprot.org/enzyme/1.8.1.4