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Literature summary for 4.1.1.81 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 4.1.1.81

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
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.
L-threonine O-3-phosphate Methanosarcina mazei
-
 (R)-1-aminopropan-2-yl phosphate + CO2
-
 ?
L-threonine O-3-phosphate Methanosarcina mazei Goe1
-
 (R)-1-aminopropan-2-yl phosphate + CO2
-
 ?

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.
L-threonine O-3-phosphate
-
 Methanosarcina mazei (R)-1-aminopropan-2-yl phosphate + CO2
-
 ?
L-threonine O-3-phosphate
-
 Methanosarcina mazei Goe1 (R)-1-aminopropan-2-yl phosphate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
CobD
-
 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 kinase, EC 2.7.1.177 Methanosarcina mazei

Cofactor

Cofactor Comment Organism Structure
4Fe-4S-center
-
 Methanosarcina mazei
pyridoxal 5'-phosphate
-
 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 cobalamin (Cbl) Methanosarcina mazei