1.1.1.88: hydroxymethylglutaryl-CoA reductase

This is an abbreviated version, for detailed information about hydroxymethylglutaryl-CoA reductase, go to the full flat file.

Reaction

(R)-mevalonate
+
CoA
+ 2 NAD+ =
3-hydroxy-3-methylglutaryl-CoA
+ 2 NADH + 2 H+

Synonyms

3-hydroxy-3-methylglutaryl CoA reductase 1, 3-hydroxy-3-methylglutaryl coenzyme A reductase, beta-hydroxy-beta-methylglutaryl CoA-reductase, beta-hydroxy-beta-methylglutaryl coenzyme A reductase, HMG-CoA reductase, hydroxymethylglutaryl coenzyme A reductase, Mt HMGR1, NADH-dependent HMG-CoA reductase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.88 hydroxymethylglutaryl-CoA reductase

Engineering

Engineering on EC 1.1.1.88 - hydroxymethylglutaryl-CoA reductase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S871A
-
150% of wild-type activity in 50 mM KCl
C156/296 A
-
fully active, resistant to N-ethylmaleimide
C156A
-
fully active, resistant to N-ethylmaleimide
C296A
-
fully active
D146A
-
6670-fold more specific for NADP+ than wild-type
D146A/L148K
-
72200-fold more specific for NADP+ than wild-type
D146A/L148R
-
83300-fold more specific for NADP+ than wild-type
D146A/Q147K
-
no activity with NADP+ as cofactor
D146A/T192K
-
no activity with NADP+ as cofactor
D146A/T192R
-
no activity with NADP+ as cofactor
D146G
-
1170-fold more specific for NADP+ than wild-type
D146G/L148K
-
55600-fold more specific for NADP+ than wild-type
D146G/L148R
-
no activity with NADP+ as cofactor
D146G/T192K
-
3170-fold more specific for NADP+ than wild-type
D146G/T192R
-
4500-fold more specific for NADP+ than wild-type
D146N
-
no activity with NADP+ as cofactor
D146S
-
no activity with NADP+ as cofactor
H381A
-
6% of wild-type activity
additional information
-
decreasing HMGR1 expression in Medicago truncatula transgenic roots by RNA interference leads to a dramatic decrease in nodulation, confirming that HMGR1 is essential for nodule development; using Medicago truncatula NORK, a receptor-like kinase, as bait in a yeast two-hybrid assay, Mt HMGR1 is identified as a NORK interacting partner. Mutagenesis and deletion analysis show that this interaction requires the cytosolic active kinase domain of NORK and the cytosolic catalytic domain of HMGR1