citrate lyase beta subunit-like protein, mitochondrial; citrate lyase beta-like; beta-methylmalate synthase (CLYBL, CLB)
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Function
- probably no ATP citrate lyase activity
- mitochondrial malate synthase
- beta-methylmalate synthase
- may play a role in vitamin B12 metabolism
acetyl-CoA + H2O + glyoxylate = (S)-malate + CoA
Propionyl-CoA + H2O + glyoxylate = beta- methylmalate + CoA
- KM=3.6 mM for glyoxylate (with acetyl-CoA as cosubstrate)
- KM=1.2 mM for glyoxylate (with propionyl-CoA as cosubstrate)
- KM=74 uM for acetyl-CoA
- KM=23 uM for propionyl-CoA
- kcat is 0.12 sec(-1) for malate synthase reaction
- kcat is 0.09 sec(-1) for beta-methylmalate synthase reaction
- binds 1 Mg+2 per subunit
Structure
- belongs to the hpcH/hpaI aldolase family, citrate lyase beta subunit-like subfamily
Compartment
Alternative splicing
named isoforms=2
Notes
- humans lack the other subunits necessary for ATP-independent citrate lyase activity
- even though CLYBL resembles citrate lyase beta subunit, it probably has a different enzyme activity