A pyridoxal-phosphate protein. This enzyme is unable to decarboxylate the D-isomer of threonine O-3-phosphate. The product of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate of EC 6.3.1.10, adenosylcobinamide-phosphate synthase, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway.
A pyridoxal-phosphate protein. This enzyme is unable to decarboxylate the D-isomer of threonine O-3-phosphate. The product of this reaction, (R)-1-aminopropan-2-yl phosphate, is the substrate of EC 6.3.1.10, adenosylcobinamide-phosphate synthase, which converts adenosylcobyric acid into adenosylcobinamide phosphate in the anaerobic cobalamin biosynthesis pathway.
adenosylcobalamin biosynthesis, end product of the corrin ring biosynthetic pathway is 5'-deoxyadenosylcobinamide phosphate, not 5'-deoxyadenosylcobinamide
bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177). Using ATP and L-Thr as substrates, the enzyme generates ADP, L-Thr-P, and (R)-1-aminopropan-2-ol O-phosphate as products. No substrate: L-serine phosphate
bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177). Using ATP and L-Thr as substrates, the enzyme generates ADP, L-Thr-P, and (R)-1-aminopropan-2-ol O-phosphate as products. No substrate: L-serine phosphate
bifunctional enzyme with L-threonine-O-3-phosphate decarboxylase (EC 4.1.1.81) and L-Thr kinase activities (EC 2.7.1.177). Using ATP and L-Thr as substrates, the enzyme generates ADP, L-Thr-P, and (R)-1-aminopropan-2-ol O-phosphate as products. No substrate: L-serine phosphate
adenosylcobalamin biosynthesis, end product of the corrin ring biosynthetic pathway is 5'-deoxyadenosylcobinamide phosphate, not 5'-deoxyadenosylcobinamide
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
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)
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)
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
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
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)
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)
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals belong to space group I222 with unit cell dimensions a : 66.6 A, b : 103.2 A, and c : 117.1 A, apo-CobD crystals belong to space group I222 with unit cell dimensions a : 76.0 A, b : 103.3 A, and c : 109.3 A
crystals grown from hanging drops, CobD crystallizes in orthorhombic space group I222, unit cell dimensions a = 67.96 A, b = 101.55 A, and c = 117.23 A
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
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
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
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
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
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
when purified under anoxic conditions, CobD displayed Michaelis-Menten kinetics and has 1000fold higher affinity for ATP and 1300fold higher catalytic efficiency than CobD purified under oxic conditions
CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2
Cheong, C.G.; Escalante-Semerena, J.C.; Rayment, I.
Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: The apo, substrate, and product-aldimine complexes