Information on EC 2.7.8.28 - 2-phospho-L-lactate transferase

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The expected taxonomic range for this enzyme is: Euryarchaeota

EC NUMBER
COMMENTARY hide
2.7.8.28
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RECOMMENDED NAME
GeneOntology No.
2-phospho-L-lactate transferase
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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
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
factor 420 biosynthesis
Methane metabolism
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Microbial metabolism in diverse environments
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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 coenzyme F420, a redox-active cofactor found in all methanogenic archaea, as well as some eubacteria.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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
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?
lactyl-2-diphospho-5'-guanosine + 7,8-didemethyl-8-hydroxy-5-deazariboflavin
guanosine 5'-phosphate + coenzyme F420-0
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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+
INHIBITORS
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, 37C
0.515
lactyl-2-diphospho-5'-adenosine
pH 7.0, 37C
0.017
lactyl-2-diphospho-5'-guanosine
pH 7.0, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34400
2 * 34400, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 34400, SDS-PAGE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
24 h, completely stable
110
30 min, complete inactivation
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S211A
mutant enzyme has the same specific activity as the wild type enzyme
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