2.7.1.177: L-threonine kinase
This is an abbreviated version!
For detailed information about L-threonine kinase, go to the full flat file.
Word Map on EC 2.7.1.177
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2.7.1.177
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enterica
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metal-binding
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adocbl
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cobamide
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mazei
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cobyric
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o-phosphate
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methanosarcina
- 2.7.1.177
- enterica
-
metal-binding
-
adocbl
- cobamide
- mazei
-
cobyric
- o-phosphate
-
methanosarcina
Reaction
Synonyms
bluE, L-Thr kinase, L-Thr kinase/L-Thr-P decarboxylase, L-Thr kinase/L-Thr-phosphate decarboxylase, MmCobD, More, PduX, RsBluE, RSP_0788
ECTree
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Metals Ions
Metals Ions on EC 2.7.1.177 - L-threonine kinase
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Ca2+
activates at low concentration, but inhibits 75% at 100 mM
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
Mg2+
additional information
a divalent metal ion (1 mM) is required for RsBluE ATPase activity, with optimal activity observed with MnCl2
additional information
enzyme CobD contains metallocenters needed for optimal activity, MmCobD is a ferroprotein
additional information
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enzyme CobD contains metallocenters needed for optimal activity, MmCobD is a ferroprotein