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Literature summary for 2.7.1.177 extracted from

  • Tavares, N.K.; Stracey, N.; Brunold, T.C.; Escalante-Semerena, J.C.
    The L-Thr kinase/l-Thr-phosphate decarboxylase (CobD) enzyme from Methanosarcina mazei Goe1 contains metallocenters needed for optimal activity (2019), Biochemistry, 58, 3260-3279 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.1.177

Protein Variants

Protein Variants Comment Organism
C434A site-directed mutagenesis, the MmCobDC434A variant has an ATPase activity that is comparable to wild-type despite having a growth phenotype similar to the DELTApduX vector control Methanosarcina mazei
C458A site-directed mutagenesis, the MmCobDC458A variant has an ATPase activity that is comparable to wild-type despite having a growth phenotype similar to the DELTApduX vector control. The mutant variant has the lowest Fe to protein ratio Methanosarcina mazei
K234A site-directed mutagenesis, the mutat variant lacks the ability to bind PLP effectively, resulting in 19 Fe per monomer, which is reduced compared to wild-type Methanosarcina mazei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Michaelis-Menten kinetics Methanosarcina mazei

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ the wild-type MmCobD that is normoxically or anoxically purified and then reconstituted, or anoxically purified without reconstitution contains an average of 25 Fe atoms per monomer, with rather poor standard deviations. The C-terminus of MmCobD contains one or more [4Fe-4S] 2+ cluster(s). Although these [4Fe-4S]2+ cluster(s) are not required for activity, perturbations in the C-terminal domain result in the loss of Fe2+ and alterations in the enzyme activities associated with the N-terminus. The C-terminus is not required for the kinase or decarboxylase activities, the [4Fe-4S]2+ cluster-containing C-terminus may have a regulatory role, perhaps by gating the active site or facilitating the decarboxylation and or kinase reactions. Fe2+ is not detected in the N-terminus only (MmCobD1-385) protein sample Methanosarcina mazei
Mg2+ required Methanosarcina mazei
additional information enzyme CobD contains metallocenters needed for optimal activity, MmCobD is a ferroprotein Methanosarcina mazei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-threonine Methanosarcina mazei
-
 ADP + O-phospho-L-threonine
-
 ?
ATP + L-threonine Methanosarcina mazei Goe1
-
 ADP + O-phospho-L-threonine
-
 ?

Organism

Organism UniProt Comment Textmining
Methanosarcina mazei Q8PVB2
-
-
Methanosarcina mazei Goe1 Q8PVB2
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-threonine
-
 Methanosarcina mazei ADP + O-phospho-L-threonine
-
 ?
ATP + L-threonine
-
 Methanosarcina mazei Goe1 ADP + O-phospho-L-threonine
-
 ?

Synonyms

Synonyms Comment Organism
L-Thr kinase
-
 Methanosarcina mazei
L-Thr kinase/L-Thr-P decarboxylase
-
 Methanosarcina mazei
L-Thr kinase/L-Thr-phosphate decarboxylase
-
 Methanosarcina mazei
MmCobD
-
 Methanosarcina mazei
More also see for L-Thr-phosphate decarboxylase, gene MM2060, EC 4.1.1.81 Methanosarcina mazei
PduX
-
 Methanosarcina mazei

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center
-
 Methanosarcina mazei
ATP
-
 Methanosarcina mazei

General Information

General Information Comment Organism
evolution the CobD protein from Methanosarcina mazei differs from other CobD homologues by the presence of a 111-amino acid cysteine-rich extended C-terminus (MmCobD386-497) annotated as a putative metal-binding domain or zinc finger protein, but it actually is a ferroprotein. This C-terminal domain is sometimes encoded as an independent protein and other times fused to other Cba biosynthetic proteins (e.g. CbiZ, CbiA, CbiH, or BtuC) Methanosarcina mazei
malfunction there is a 2600fold decrease in catalytic efficiency (kcat/Km) when the C-terminus is removed, or a 1200fold decrease when the enzyme is purified normoxically Methanosarcina mazei
additional information MmCobD displays redox-sensitivity Methanosarcina mazei
physiological function MmCobD is a bifunctional enzyme with L-threonine (L-Thr) kinase (PduX, EC 2.7.1.177) and pyridoxal 5'-phosphate (PLP)-dependent L-threonine phosphate (L-Thr-P) decarboxylase activities needed to synthesize the (R)-1-amino-propan-2-ol O-phosphate (a.k.a. (R)-1-amino-2-propanol-O-2-phosphate, AP-P) moiety of cobalamine (Cbl) Methanosarcina mazei