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- **********************************************************
- * ATP-citrate lyase and succinyl-CoA ligases active site *
- **********************************************************
-
- Three different enzymes share a similar catalytic mechanism which involves the
- phosphorylation by ATP (or GTP) of a specific histidine residue in the active
- site. These enzymes are:
-
- - ATP citrate-lyase (EC 4.1.3.8) [1], the primary enzyme responsible for the
- synthesis of cytosolic acetyl-CoA in many tissues, catalyzes the formation
- of acetyl-CoA and oxaloacetate from citrate and CoA with the concomitant
- hydrolysis of ATP to ADP and phosphate. ATP-citrate lyase is a tetramer of
- identical subunits.
- - Succinyl-CoA ligase (GDP-forming) (EC 6.2.1.4) [2] is a mitochondrial
- enzyme that catalyzes the substrate level phosphorylation step of the
- tricarboxylic acid cycle: the formation of succinyl-CoA from succinate with
- a concomitant hydrolysis of GTP to GDP and phosphate. This enzyme is a
- dimer composed of an alpha and a beta subunits.
- - Succinyl-CoA ligase (ADP-forming) (EC 6.2.1.5) [3] is a bacterial enzyme
- that during aerobic metabolism functions in the citric acid cycle, coupling
- the hydrolysis of succinyl-CoA to the synthesis of ATP. It can also
- function in the other direction for anabolic purposes. This enzyme is a
- tetramer composed of two alpha and two beta subunits.
-
- The region around the phosphorylated histidine residues in these three enzymes
- is well conserved and can be used as a signature pattern.
-
- -Consensus pattern: [LIVMF]-G-H-A-G-A
- [H is the phosphorylated active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: human cytomegalovirus hypothetical
- protein UL49.
- -Last update: November 1990 / First entry.
-
- [ 1] Elshourbagy N.A., Near J.C., Kmetz P.J., Sathe G.M., Southan C.,
- Strickler J.E., Gross M., Young J.F., Wells T.N.C., Groot P.H.E.
- J. Biol. Chem. 265:1430-1435(1990).
- [ 2] Henning W.D., Upton C., Mcfadden G., Majumdar R., Bridger W.A.
- Proc. Natl. Acad. Sci. U.S.A. 85:1432-1436(1988).
- [ 3] Buck D., Spencer M.E., Guest J.R.
- Biochemistry 24:6245-6252(1985).
-