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Information on EC 2.7.8.28 - 2-phospho-L-lactate transferase and Organism(s) Methanosarcina mazei and UniProt Accession Q8PVT6

for references in articles please use BRENDA:EC2.7.8.28
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EC Tree
IUBMB Comments
This enzyme is involved in the biosynthesis of factor 420, a redox-active cofactor, in methanogenic archaea and certain bacteria. The specific reaction catalysed in vivo is determined by the availability of substrate, which in turn is determined by the enzyme present in the organism - EC 2.7.7.68, 2-phospho-L-lactate guanylyltransferase, EC 2.7.7.105, phosphoenolpyruvate guanylyltransferase, or EC 2.7.7.106, 3-phospho-D-glycerate guanylyltransferase.
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This record set is specific for:
Methanosarcina mazei
UNIPROT: Q8PVT6
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The taxonomic range for the selected organisms is: Methanosarcina mazei
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
mj1256, 2-phospho-l-lactate transferase, lppg:fo 2-phospho-l-lactate transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2-phospho-L-lactate transferase
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CofD
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fbiA
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lactyl-2-diphospho-(5')guanosine:Fo 2-phospho-L-lactate transferase
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LPPG:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase
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LPPG:Fo 2-phospho-L-lactate transferase
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SYSTEMATIC NAME
IUBMB Comments
(2S)-lactyl-2-diphospho-5'-guanosine:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase
This enzyme is involved in the biosynthesis of factor 420, a redox-active cofactor, in methanogenic archaea and certain bacteria. The specific reaction catalysed in vivo is determined by the availability of substrate, which in turn is determined by the enzyme present in the organism - EC 2.7.7.68, 2-phospho-L-lactate guanylyltransferase, EC 2.7.7.105, phosphoenolpyruvate guanylyltransferase, or EC 2.7.7.106, 3-phospho-D-glycerate guanylyltransferase.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin
guanosine 5'-phosphate + coenzyme F420-0
show the reaction diagram
the reaction is the fourth step in the biosynthesis of coenzyme F420
coenzyme F420-0 is coenzyme F420 without glutamic acid
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin
guanosine 5'-phosphate + coenzyme F420-0
show the reaction diagram
the reaction is the fourth step in the biosynthesis of coenzyme F420
coenzyme F420-0 is coenzyme F420 without glutamic acid
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of the CofD enzyme, in its free form at 3.1 A resolution, in a ternary complex with 7,8-didemethyl-8-hydroxy-5-deazaflavin and phosphate at 2.5 A resolution, and in a ternary complex with 7,8-didemethyl-8-hydroxy-5-deazaflavin and GDP at 3.0 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Forouhar, F.; Abashidze, M.; Xu, H.; Grochowski, L.L.; Seetharaman, J.; Hussain, M.; Kuzin, A.; Chen, Y.; Zhou, W.; Xiao, R.; Acton, T.B.; Montelione, G.T.; Galinier, A.; White, R.H.; Tong, L.
Molecular insights into the biosynthesis of the F420 coenzyme
J. Biol. Chem.
283
11832-11840
2008
Methanosarcina mazei (Q8PVT6), Methanosarcina mazei
Manually annotated by BRENDA team