Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.4.4.2 - glycine dehydrogenase (aminomethyl-transferring)

for references in articles please use BRENDA:EC1.4.4.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A pyridoxal-phosphate protein. A component of the glycine cleavage system, which 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, aminomethyltransferase), the L protein (EC 1.8.1.4, dihydrolipoyl dehydrogenase) and the lipoyl-bearing H protein . Previously known as glycine synthase.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
UNIPROT: P25855
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
gdc, h protein, h-protein, glycine decarboxylase, t protein, protein p1, h1 protein, glycine decarboxylase complex, glycine cleavage enzyme complex, h2 protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Gly decarboxylase H1
-
glycine cleavage system H protein 1
-
glycine decarboxylase complex
-
glycine decarboxylase complex H
-
decarboxylase, glycine
-
-
-
-
Glycine cleavage system P-protein
-
-
-
-
glycine decarboxylase
-
-
-
-
glycine decarboxylase P-protein
-
-
-
-
glycine dehydrogenase (decarboxylating)
-
-
-
-
glycine-cleavage complex
-
-
-
-
P-protein
-
-
-
-
Protein P1
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
-
-
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
glycine:H-protein-lipoyllysine oxidoreductase (decarboxylating, acceptor-amino-methylating)
A pyridoxal-phosphate protein. A component of the glycine cleavage system, which 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, aminomethyltransferase), the L protein (EC 1.8.1.4, dihydrolipoyl dehydrogenase) and the lipoyl-bearing H protein [3]. Previously known as glycine synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
37259-67-9
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis-(2-nitrobenzoic acid)
complete inhibition
aminoacetonitrile
the inhibitor of GDC is able to mimic mitochondrial depolarization, hydrogen peroxide production, and cell death in response to stress or harpin treatment of cultured Arabidopsis cells
harpin
the bacterial elicitor, a strong inducer of reactive oxygen species and NO, inhibits GDC activity
-
N-ethylmaleimide
complete inhibition
S-nitrosoglutathione
i.e. GSNO, the glycine decarboxylase complex, GDC activity is inhibited by S-nitrosoglutathione due to S-nitrosylation/S-glutathionylation of several cysteine residues, overview. The inhibition of GDC activity after GSNO treatment can be an indirect effect of ROS induced by inhibition of complex I
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the glycine decarboxylase complex, GDC, is a key enzyme of the photorespiratory C2 cycle in C3 plants, regulation of plant glycine decarboxylase by S-nitrosylation and glutathionylation, overview. GDC activity is inhibited by S-nitrosoglutathione due to S-nitrosylation/S-glutathionylation of several cysteine residues
physiological function
role of GDC in the harpin-induced plant defense response, overview
additional information
the mitochondrial photorespiratory system is involved in the regulation of NO signal transduction in Arabidopsis thaliana
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GCSH1_ARATH
165
0
17947
Swiss-Prot
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
peptide mapping using trypsin degestion, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Palmieri, M.C.; Lindermayr, C.; Bauwe, H.; Steinhauser, C.; Durner, J.
Regulation of plant glycine decarboxylase by s-nitrosylation and glutathionylation
Plant Physiol.
152
1514-1528
2010
Arabidopsis thaliana (P25855)
Manually annotated by BRENDA team