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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Enzyme: (R)-citramalate synthase

Gene: cimA Accession Number: G-9230 (MetaCyc)

Synonyms: LA2350

Species: Leptospira interrogans serovar Lai str. 56601

Subunit composition of (R)-citramalate synthase = [CimA]2
         (R)-citramalate synthase subunit = CimA

Summary:
(R)-citramalate synthase from Leptospira interrogans serovar Lai str. 56601 has been cloned and expressed in Escherichia coli [Xu04d]. The specific activity was 2.53 μmol/min/mg of protein under standard conditions. Kcat of the enzyme was 2.41 s-1. Activity was very specific towards pyruvate, with no detectible activity towards any other keto acid substrates.
This gene was incorrectly predicted to encode an α-isopropylmalate synthase. It was later shown to encode an (R)-citramalate synthase [Xu04d].

Gene Citations: [Ren03]

Molecular Weight of Polypeptide: 57.319 kD (from nucleotide sequence), 57 kD (experimental) [Xu04d ]

Unification Links: Entrez-gene:1151693 , ModBase:Q8F3Q1 , Protein Model Portal:Q8F3Q1 , Swiss-Model:Q8F3Q1 , UniProt:Q8F3Q1

Relationship Links: Entrez-Nucleotide:RELATED-TO:AE010300 , InterPro:IN-FAMILY:IPR000891 , InterPro:IN-FAMILY:IPR002034 , InterPro:IN-FAMILY:IPR013709 , InterPro:IN-FAMILY:IPR013785 , PDB:Structure:3BLE , PDB:Structure:3BLF , PDB:Structure:3BLI , PDB:Structure:3F6G , PDB:Structure:3F6H , Pfam:IN-FAMILY:PF00682 , Pfam:IN-FAMILY:PF08502 , Prosite:IN-FAMILY:PS00815 , Prosite:IN-FAMILY:PS50991 , Smart:IN-FAMILY:SM00917

Gene-Reaction Schematic: ?


Enzymatic reaction of: (R)-citramalate synthase

EC Number: 2.3.1.182

acetyl-CoA + pyruvate + H2O <=> (R)-citramalate + coenzyme A + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: isoleucine biosynthesis II

Inhibitors (Allosteric): L-isoleucine [Xu04d]

Inhibitors (Unknown Mechanism): 1H-imidazole [Xu04d]

Primary Physiological Regulators of Enzyme Activity: L-isoleucine

Kinetic Parameters:

Substrate
Km (μM)
Citations
pyruvate
43.0
[Xu04d]

T(opt): 37 °C [Xu04d]


References

Ren03: Ren SX, Fu G, Jiang XG, Zeng R, Miao YG, Xu H, Zhang YX, Xiong H, Lu G, Lu LF, Jiang HQ, Jia J, Tu YF, Jiang JX, Gu WY, Zhang YQ, Cai Z, Sheng HH, Yin HF, Zhang Y, Zhu GF, Wan M, Huang HL, Qian Z, Wang SY, Ma W, Yao ZJ, Shen Y, Qiang BQ, Xia QC, Guo XK, Danchin A, Saint Girons I, Somerville RL, Wen YM, Shi MH, Chen Z, Xu JG, Zhao GP (2003). "Unique physiological and pathogenic features of Leptospira interrogans revealed by whole-genome sequencing." Nature 422(6934);888-93. PMID: 12712204

Xu04d: Xu, H., Zhang, Y., Guo, X., Ren, S., Staempfli, A.A., Chiao, J., Jiang, W., Zhao, G. (2004). "Isoleucine biosynthesis in Leptospira interrogans serotype lai strain 56601 proceeds via a threonine-independent pathway." J. Bacteriol. 186(16):5400-5409. PMID: 15292141


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sun Dec 21, 2014, BIOCYC13A.