Disease relevance of fumC

• Primers specific for Escherichia coli O15:K52:H1 were devised based on a novel single-nucleotide polymorphism identified within the housekeeping gene fumC, i.e., G594A [1].
• Fumarase C activity is elevated in response to iron deprivation and in mucoid, alginate-producing Pseudomonas aeruginosa: cloning and characterization of fumC and purification of native fumC [2].

High impact information on fumC

• The multisubunit active site of fumarase C from Escherichia coli [3].
• Fumarase C, the stable fumarase of Escherichia coli, is controlled by the soxRS regulon [4].
• These results indicate that fumarase C is a member of the soxRS regulon and that this regulon does not respond to changes in O2- concentration but perhaps does respond to some consequence of a decrease in the ratio of NADPH to NADP+ [4].
• The overall folding of the present enzyme subunit is similar to those of the E.coli aspartase and the E.coli fumarase C, both of which belong to the same superfamily as the present enzyme [5].
• Fumarase C purified from Escherichia coli has been crystallized in the presence of polyethylene glycol in both a citrate buffer at pH 5.3 and a 3-(4-morpholino)-propanesulfonic acid buffer at pH 7.5 yielding two crystal forms [6].

Chemical compound and disease context of fumC

• In this study, the argininosuccinate substrate was modeled into the active site of duck delta IotaIota crystallin, using the coordinates of an inhibitor-bound Escherichia coli fumarase C structure to orient the fumarate moiety of the substrate [7].
• A homology search for the products deduced from the sequenced data revealed that the orf H exhibited high similarity to malic acid enzyme of Haemophilus influenzae and fumarate hydratase of Escherichia coli (orf J) [8].
• Previous crystal structures of fumarase C from Escherichia coli have noted two occupied dicarboxylate-binding sites termed the active site and the B site [9].
• In superoxide dismutase-deficient E. coli mutants, glycolaldehyde induces fumarase C and nitroreductase A, which are regulated as members of the soxRS regulon [10].

Biological context of fumC

• Typical archaebacterial regulatory sites were identified in the region flanking the fumC open reading frame [11].
• SoxR completely inhibited the migration of a DNA fragment containing the promoter region of fumC, in gel-shift experiments [12].
• While the fumA and fumC gene products are expressed under aerobic cell growth conditions, the FumB fumarase appears to be more abundant during anaerobic growth [13].
• Class II contains fumarase C and porcine fumarase, which have amino acid sequences 60% identical to each other [Woods, S.A., Schwartzbach, S.D., & Guest, J.R. (1988) Biochim. Biophys. Acta 954, 14-26] [14].
• In addition, the iron-regulated, tricarboxylic acid cycle enzyme fumarase C is essential for optimal alginate production by P. aeruginosa [2].

Anatomical context of fumC

• PCR primers specific for the recently described antimicrobial resistance-associated Escherichia coli clonal group A (CGA), a widespread cause of drug-resistant urinary tract infections in the United States, were devised on the basis of a novel single-nucleotide polymorphism identified within the housekeeping gene fumC, i.e., C288T [15].

Associations of fumC with chemical compounds

• Fumarase C catalyzes the stereospecific interconversion of fumarate to L-malate as part of the metabolic citric acid or Kreb's cycle [16].
• L-aspartate ammonia-lyase and fumarate hydratase share extensive sequence homology [17].
• The importance of Fe(II) for the unstable fumarases was exposed by alpha,alpha'-dipyridyl, which decreased fumarases A + B without affecting fumarase C or the inductive effect thereon of paraquat [18].

Analytical, diagnostic and therapeutic context of fumC

• Amino acid and N-terminal sequence analyses supported the possibility that the enzyme is a product of fumC gene (FUMC) [19].
• Purification and crystallization of fumarase C from Escherichia coli [6].
• To more fully understand the implications of this mutation, a single-step site-directed mutagenesis method was used to generate the homologous substitution at position 315 within fumarase C from Escherichia coli [20].

References