Citrate lyase
Citrate lyase structure
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Common Name | Citrate lyase | ||
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| CAS Number | 9012-83-3 | Molecular Weight | N/A | |
| Density | N/A | Boiling Point | N/A | |
| Molecular Formula | N/A | Melting Point | N/A | |
| MSDS | USA | Flash Point | N/A | |
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A novel ATP-generating machinery to counter nitrosative stress is mediated by substrate-level phosphorylation.
Biochim. Biophys. Acta 1850(1) , 43-50, (2015) It is well-known that elevated amounts of nitric oxide and other reactive nitrogen species (RNS) impact negatively on the tricarboxylic acid (TCA) cycle and oxidative phosphorylation. These perturbations severely compromise O2-dependent energy production. Whi... |
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Acid-inducible transcription of the operon encoding the citrate lyase complex of Lactococcus lactis Biovar diacetylactis CRL264.
J. Bacteriol. 186(17) , 5649-60, (2004) Although Lactococcus is one of the most extensively studied lactic acid bacteria and is the paradigm for biochemical studies of citrate metabolism, little information is available on the regulation of the citrate lyase complex. In order to fill this gap, we c... |
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Identification of the active site of phosphoribosyl-dephospho-coenzyme A transferase and relationship of the enzyme to an ancient class of nucleotidyltransferases.
Biochemistry 39(43) , 13233-40, (2000) Malonate decarboxylase from Klebsiella pneumoniae contains an acyl carrier protein (MdcC) to which a 2'-(5' '-phosphoribosyl)-3'-dephospho-CoA prosthetic group is attached via phosphodiester linkage to serine 25. We have shown in the preceding paper in this i... |
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Biosynthesis of the prosthetic group of citrate lyase.
Biochemistry 39(31) , 9438-50, (2000) Citrate lyase (EC 4.1.3.6) catalyzes the cleavage of citrate to acetate and oxaloacetate and is composed of three subunits (alpha, beta, and gamma). The gamma-subunit serves as an acyl carrier protein (ACP) and contains the prosthetic group 2'-(5' '-phosphori... |
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Identification of a gene cluster in Klebsiella pneumoniae which includes citX, a gene required for biosynthesis of the citrate lyase prosthetic group.
J. Bacteriol. 184(9) , 2439-46, (2002) The biosynthesis of the 2'-(5"-phosphoribosyl)-3'-dephospho-coenzyme A (CoA) prosthetic group of citrate lyase (EC 4.1.3.6), a key enzyme of citrate fermentation, proceeds via the initial formation of the precursor 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA a... |
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A turn-on fluorescent indicator for citrate with micromolar sensitivity.
Dalton Trans. (36) , 4027-33, (2007) A turn-on fluorescent indicator for citric acid (citrate) has been developed, displaying high emission enhancement (+1500%) and low interference by other carboxylates. The sensor is based on the non-emissive copper(II) complex of a fluorescent amino amide, wh... |
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Characterization of the isolated transferase subunit of citrate lyase as a CoA-Transferase. Evidence against a covalent enzyme-substrate intermediate.
Eur. J. Biochem. 80(2) , 479-88, (1977)
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The structure and computational analysis of Mycobacterium tuberculosis protein CitE suggest a novel enzymatic function.
J. Mol. Biol. 365(2) , 275-83, (2007) Fatty acid biosynthesis is essential for the survival of Mycobacterium tuberculosis and acetyl-coenzyme A (acetyl-CoA) is an essential precursor in this pathway. We have determined the 3-D crystal structure of M. tuberculosis citrate lyase beta-subunit (CitE)... |
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Structural insights into RipC, a putative citrate lyase β subunit from a Yersinia pestis virulence operon.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68(Pt 1) , 2-7, (2012) Yersinia pestis remains a threat, with outbreaks of plague occurring in rural areas and its emergence as a weapon of bioterrorism; thus, an improved understanding of its various pathogenicity pathways is warranted. The rip (required for intracellular prolifer... |
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Genetic organization of the citCDEF locus and identification of mae and clyR genes from Leuconostoc mesenteroides.
J. Bacteriol. 181(14) , 4411-6, (1999) In this paper, we describe two open reading frames coding for a NAD-dependent malic enzyme (mae) and a putative regulatory protein (clyR) found in the upstream region of citCDEFG of Leuconostoc mesenteroides subsp. cremoris 195. The transcriptional analysis o... |