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Literature summary extracted from

  • Giffhorn, F.; Gottschalk, G.
    Inactivation of citrate lyase from Rhodopseudomonas gelatinosa by a specific deacetylase and inhibition of this inactivation by L-(+)-glutamate (1975), J. Bacteriol., 124, 1052-1061.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.2.16 citrate induced by Rubrivivax gelatinosus

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.2.16 EDTA 0.01 M, 40% inhibition Rubrivivax gelatinosus
3.1.2.16 L-arginine 0.01 M, 47% inhibition Rubrivivax gelatinosus
3.1.2.16 L-aspartate
-
 Rubrivivax gelatinosus
3.1.2.16 L-glutamate
-
 Rubrivivax gelatinosus
3.1.2.16 additional information D-glutamate, 2-oxoglutarate, L-alpha-hydroxyglutarate and L-proline are less effective inhibitors, iodoacetate, iodoacetamide or N-ethylmaleimide does not interfere with deacetylase activity Rubrivivax gelatinosus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.1.2.16 0.0001
-
 [citrate (pro-3S)-lyase](acetyl form) pH 7.2, 30°C Rubrivivax gelatinosus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.2.16 [citrate (pro-3S)-lyase](acetyl form) + H2O Rubrivivax gelatinosus
-
 [citrate (pro-3S)-lyase](thiol form) + acetate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.2.16 no activity in Enterobacter aerogenes
-
-
-
3.1.2.16 no activity in Streptococcus diacetilactis
-
-
-
3.1.2.16 Rubrivivax gelatinosus
-
 DSM 149
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.2.16
-
 Rubrivivax gelatinosus

Storage Stability

EC Number Storage Stability Organism
3.1.2.16 -15°C, purified enzyme stable for at least 6 months Rubrivivax gelatinosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.2.16 additional information acetyl-CoA, acetoacetyl-CoA, S-acetyl-N-acetylcyseamine and purified citrate lyases from Enterobacter aerogenes and Streptococcus diacetilactis are no substrates, reaction with butyryl-S-citrate lyase, propionyl-S-citrate lyaseand acetyl-S-citrate lyase only slightly faster than spontaneous hydrolysis Rubrivivax gelatinosus ?
-
 ?
3.1.2.16 [citrate (pro-3S)-lyase](acetyl form) + H2O
-
 Rubrivivax gelatinosus [citrate (pro-3S)-lyase](thiol form) + acetate
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.2.16 8.1
-
-
 Rubrivivax gelatinosus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.2.16 7.2 8.1 because of the instability of the substrate acetyl-S-citrate lyase at acidic and alkaline pH-values, all assays are carried out at pH 7.2, where the spontanous hydrolysis of the substrate is negligible and the enzyme shows 70% of the activity at pH 8.1 Rubrivivax gelatinosus