Biotin-independent malonate decarboxylase

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Biotin-independent malonate decarboxylase
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EC no. 4.1.1.88
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Biotin-independent malonate decarboxylase (EC 4.1.1.88, malonate decarboxylase (without biotin), malonate decarboxylase, MDC) is an enzyme with systematic name malonate carboxy-lyase (biotin-independent). [1] [2] [3] [4] [5] [6] [7] [8] [9] This enzyme catalyses the following chemical reaction

malonate + H+ acetate + CO2

Two types of malonate decarboxylase are currently known, both of which form multienzyme complexes.

Related Research Articles

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In enzymology, a methylmalonyl-CoA carboxytransferase is an enzyme that catalyzes the chemical reaction

The enzyme citramalyl-CoA lyase catalyzes the chemical reaction

<span class="mw-page-title-main">Methylmalonyl-CoA decarboxylase</span>

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<span class="mw-page-title-main">ATP citrate synthase</span> Class of enzymes

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<span class="mw-page-title-main">Morpheein</span> Model of protein allosteric regulation

Morpheeins are proteins that can form two or more different homo-oligomers, but must come apart and change shape to convert between forms. The alternate shape may reassemble to a different oligomer. The shape of the subunit dictates which oligomer is formed. Each oligomer has a finite number of subunits (stoichiometry). Morpheeins can interconvert between forms under physiological conditions and can exist as an equilibrium of different oligomers. These oligomers are physiologically relevant and are not misfolded protein; this distinguishes morpheeins from prions and amyloid. The different oligomers have distinct functionality. Interconversion of morpheein forms can be a structural basis for allosteric regulation, an idea noted many years ago, and later revived. A mutation that shifts the normal equilibrium of morpheein forms can serve as the basis for a conformational disease. Features of morpheeins can be exploited for drug discovery. The dice image represents a morpheein equilibrium containing two different monomeric shapes that dictate assembly to a tetramer or a pentamer. The one protein that is established to function as a morpheein is porphobilinogen synthase, though there are suggestions throughout the literature that other proteins may function as morpheeins.

<span class="mw-page-title-main">Group II pyridoxal-dependent decarboxylases</span> Class of enzymes

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<span class="mw-page-title-main">Diacetyl reductase ((S)-acetoin forming)</span>

Diacetyl reductase ((S)-acetoin forming) (EC 1.1.1.304, (S)-acetoin dehydrogenase) is an enzyme with systematic name (S)-acetoin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

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Malonyl CoA reductase (malonate semialdehyde-forming) (EC 1.2.1.75, NADP-dependent malonyl CoA reductase, malonyl CoA reductase (NADP)) is an enzyme with systematic name malonate semialdehyde:NADP+ oxidoreductase (malonate semialdehyde-forming). This enzyme catalyse the following chemical reaction

Catalase-peroxidase (EC 1.11.1.21, katG (gene)) is an enzyme with systematic name donor:hydrogen-peroxide oxidoreductase. This enzyme catalyses the following chemical reaction

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Malonyl-S-ACP:biotin-protein carboxyltransferase is an enzyme with systematic name malonyl-(acyl-carrier protein):biotinyl-(protein) carboxytransferase. This enzyme catalyses the following chemical reaction

Acetyl-S-ACP:malonate ACP transferase is an enzyme with systematic name acetyl-(acyl-carrier-protein):malonate S-(acyl-carrier-protein)transferase. This enzyme catalyses the following chemical reaction

Malonate decarboxylase holo-(acyl-carrier protein) synthase is an enzyme with systematic name 2'-(5-triphosphoribosyl)-3'-dephospho-CoA:apo-malonate-decarboxylase 2'-(5-phosphoribosyl)-3'-dephospho-CoA-transferase . This enzyme catalyses the following chemical reaction

Malonyl-S-ACP decarboxylase (EC 4.1.1.87, malonyl-S-acyl-carrier protein decarboxylase, MdcD/MdcE, MdcD,E) is an enzyme with systematic name malonyl-(acyl-carrier-protein) carboxy-lyase. This enzyme catalyses the following chemical reaction

Biotin-dependent malonate decarboxylase (EC 4.1.1.89, malonate decarboxylase (with biotin), malonate decarboxylase) is an enzyme with systematic name malonate carboxy-lyase (biotin-dependent). This enzyme catalyses the following chemical reaction

Carboxybiotin decarboxylase (EC 7.2.4.1, MadB, carboxybiotin protein decarboxylase) is an enzyme with systematic name carboxybiotinyl-(protein) carboxy-lyase. This enzyme catalyses the following chemical reaction

Acetate—[acyl-carrier protein] ligase is an enzyme with systematic name acetate:(acyl-carrier-protein) ligase (AMP-forming). This enzyme catalyses the following chemical reaction

The Na+-transporting Carboxylic Acid Decarboxylase (NaT-DC) Family (TC# 3.B.1) is a family of porters that belong to the CPA superfamily. Members of this family have been characterized in both Gram-positive and Gram-negative bacteria. A representative list of proteins belonging to the NaT-DC family can be found in the Transporter Classification Database.

References

  1. ↑ Schmid M, Berg M, Hilbi H, Dimroth P (April 1996). "Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic group". European Journal of Biochemistry. 237 (1): 221–8. doi:10.1111/j.1432-1033.1996.0221n.x. PMID   8620876.
  2. ↑ Byun, H.S.; Kim, Y.S. (1997). "Subunit organization of bacterial malonate decarboxylases: the smallest δ subunit as an acyl-carrier protein". J. Biochem. Mol. Biol. 30: 132–137.
  3. ↑ Hoenke S, Schmid M, Dimroth P (June 1997). "Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli". European Journal of Biochemistry. 246 (2): 530–8. doi: 10.1111/j.1432-1033.1997.00530.x . PMID   9208947.
  4. ↑ Chohnan S, Fujio T, Takaki T, Yonekura M, Nishihara H, Takamura Y (December 1998). "Malonate decarboxylase of Pseudomonas putida is composed of five subunits". FEMS Microbiology Letters. 169 (1): 37–43. doi: 10.1111/j.1574-6968.1998.tb13296.x . PMID   9851033.
  5. ↑ Hoenke S, Schmid M, Dimroth P (October 2000). "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. doi:10.1021/bi001154u. PMID   11052676.
  6. ↑ Handa S, Koo JH, Kim YS, Floss HG (October 1999). "Stereochemical course of biotin-independent malonate decarboxylase catalysis". Archives of Biochemistry and Biophysics. 370 (1): 93–6. doi:10.1006/abbi.1999.1369. PMID   10496981.
  7. ↑ Koo JH, Kim YS (December 1999). "Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus". European Journal of Biochemistry. 266 (2): 683–90. doi: 10.1046/j.1432-1327.1999.00924.x . PMID   10561613.
  8. ↑ Kim YS (September 2002). "Malonate metabolism: biochemistry, molecular biology, physiology, and industrial application". Journal of Biochemistry and Molecular Biology. 35 (5): 443–51. doi: 10.5483/bmbrep.2002.35.5.443 . PMID   12359084.
  9. ↑ Dimroth P, Hilbi H (July 1997). "Enzymic and genetic basis for bacterial growth on malonate". Molecular Microbiology. 25 (1): 3–10. doi: 10.1046/j.1365-2958.1997.4611824.x . PMID   11902724.
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