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Information on EC 2.7.8.28 - 2-phospho-L-lactate transferase and Organism(s) Methanocaldococcus jannaschii and UniProt Accession Q58653

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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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Methanocaldococcus jannaschii
UNIPROT: Q58653
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The taxonomic range for the selected organisms is: Methanocaldococcus jannaschii
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
-
lactyl-2-diphospho-(5')guanosine:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase
-
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
-
LPPG:Fo 2-phospho-L-lactate transferase
-
CofD
-
-
-
-
fbiA
-
-
-
-
lactyl-2-diphospho-(5')guanosine:Fo 2-phospho-L-lactate transferase
-
-
-
-
LPPG:7,8-didemethyl-8-hydroxy-5-deazariboflavin 2-phospho-L-lactate transferase
-
-
-
-
LPPG:Fo 2-phospho-L-lactate transferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2S)-lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin = GMP + coenzyme F420-0
show the reaction diagram
coenzyme F420-0 is coenzyme F420 without glutamic acid
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'-adenosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin
adenosine 5'-phosphate + coenzyme F420-0
show the reaction diagram
catalysis does not appear to proceed via a covalent intermediate
coenzyme F420-0 is coenzyme F420 without glutamic acid
-
?
lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin
guanosine 5'-phosphate + coenzyme F420-0
show the reaction diagram
additional information
?
-
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
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
isolated CofD enzyme is not activated by the addition of 0-4 mM MgCl2. The inactivation by EDTA can be completely reversed by the addition of excess Mg2+ but not by the addition of Zn2+ or Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032
7,8-didemethyl-8-hydroxy-5-deazariboflavin
pH 7.0, 37°C
0.515
lactyl-2-diphospho-5'-adenosine
pH 7.0, 37°C
0.017
lactyl-2-diphospho-5'-guanosine
pH 7.0, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34400
2 * 34400, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 34400, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S211A
mutant enzyme has the same specific activity as the wild type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110
30 min, complete inactivation
80
24 h, completely stable
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
Graupner, M.; Xu, H.; White, R.H.
Characterization of the 2-phospho-L-lactate transferase enzyme involved in coenzyme F(420) biosynthesis in Methanococcus jannaschii
Biochemistry
41
3754-3761
2002
Methanocaldococcus jannaschii (Q58653), Methanocaldococcus jannaschii
Manually annotated by BRENDA team