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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: C5APL4
• Protein Description: SubName: Full=Malonate decarboxylase, beta-subunit {ECO:0000313|EMBL:ACS37998.1}; EC=6.4.1.3 {ECO:0000313|EMBL:ACS37998.1};
• Gene Information: Name=mdcD {ECO:0000313|EMBL:ACS37998.1}; OrderedLocusNames=MexAM1_META1p0025 {ECO:0000313|EMBL:ACS37998.1};
• Organism (full): Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens).
• Protein Family: Not specified in UniProt
• Key Domains: AcCoA_carboxyl_beta. (IPR034733); ClpP/crotonase-like_dom_sf. (IPR029045); COA_CT_N. (IPR011762); Malonate_beta. (IPR017556); Carboxyl_trans (PF01039)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "mdcD" matches the protein description above
2. Verify the organism is correct: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'mdcD' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene mdcD (gene ID: mdcD, UniProt: C5APL4) in METEA.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: C5APL4
• Protein Description: SubName: Full=Malonate decarboxylase, beta-subunit {ECO:0000313|EMBL:ACS37998.1}; EC=6.4.1.3 {ECO:0000313|EMBL:ACS37998.1};
• Gene Information: Name=mdcD {ECO:0000313|EMBL:ACS37998.1}; OrderedLocusNames=MexAM1_META1p0025 {ECO:0000313|EMBL:ACS37998.1};
• Organism (full): Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens).
• Protein Family: Not specified in UniProt
• Key Domains: AcCoA_carboxyl_beta. (IPR034733); ClpP/crotonase-like_dom_sf. (IPR029045); COA_CT_N. (IPR011762); Malonate_beta. (IPR017556); Carboxyl_trans (PF01039)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "mdcD" matches the protein description above
2. Verify the organism is correct: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens).
3. Check if protein family/domains align with what you find in literature
4. If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'mdcD' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene mdcD (gene ID: mdcD, UniProt: C5APL4) in METEA.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Plan
- Verified target identity and organism: The query concerns mdcD (UniProt C5APL4), annotated as the beta subunit of malonate decarboxylase in Methylorubrum (Methylobacterium) extorquens AM1; domain annotations (carboxyltransferase beta/carboxyl_trans PF01039; crotonase-like fold; COA_CT_N) align with literature on the malonate decarboxylase carboxyltransferase (MdcD–MdcE) family (see Key concepts). (hoenke1997sequenceofa pages 1-2, hoenke1997sequenceofa pages 4-5, maderbocus2017crystalstructureof pages 1-2, maderbocus2017crystalstructureof pages 2-4)
- Collected authoritative structural/biochemical sources for MDC and MdcD–MdcE, plus operon organization and ACP prosthetic chemistry. (maderbocus2017crystalstructureof pages 1-2, maderbocus2017crystalstructureof pages 2-4, dimroth1997enzymicandgenetic pages 4-6, hoenke1997sequenceofa pages 1-2, hoenke1997sequenceofa pages 4-5, chohnan2004malonatedecarboxylasein pages 2-4)
- Assessed organism-specific evidence; direct AM1 experimental reports were not found in the retrieved set. Operon presence and function for AM1 are inferred by strong homology and conserved gene synteny seen across bacteria; we note this as a limitation. (hoenke1997sequenceofa pages 1-2, chohnan2004malonatedecarboxylasein pages 2-4)
- Prioritized most recent high-impact structural work (2017) and summarized developments; few post-2017 primary advances were retrieved in this search scope, which we note explicitly. (maderbocus2017crystalstructureof pages 1-2, maderbocus2017crystalstructureof pages 2-4, maderbocus2017crystalstructureof pages 10-10)

Comprehensive research report

1) Key concepts and definitions with current understanding
- Malonate decarboxylase (MDC): A bacterial enzyme system for growth on malonate that catalyzes decarboxylation of malonyl groups to acetyl groups with CO2 release. Two MDC categories exist: a biotin-dependent, membrane-associated enzyme that couples decarboxylation to Na+ translocation, and a biotin-independent, soluble multi-subunit complex found in many aerobes. The biotin-independent form comprises at minimum MdcA (acetyl-ACP:malonate ACP transferase), MdcC (an acyl carrier protein with an unusual prosthetic group), and the carboxyltransferase pair MdcD–MdcE that decarboxylates malonyl-ACP to regenerate acetyl-ACP. Accessory proteins include a malonyl-CoA:ACP transacylase (MdcH) and genes for prosthetic-group biosynthesis and transport/regulation (e.g., MdcB, MdcG, MdcF, MdcR). (Dimroth & Hilbi 1997, Mol Microbiol; Hoenke et al. 1997, Eur J Biochem; Chohnan & Takamura 2004, Microbes Environ; Maderbocus et al. 2017, Nat Commun) (dimroth1997enzymicandgenetic pages 4-6, hoenke1997sequenceofa pages 1-2, hoenke1997sequenceofa pages 4-5, chohnan2004malonatedecarboxylasein pages 2-4, maderbocus2017crystalstructureof pages 1-2)
- MdcD (beta subunit): The beta subunit of the MDC carboxyltransferase that partners with MdcE (gamma subunit) to form the malonyl-ACP decarboxylase active site. Sequence and structure place MdcD in the carboxyltransferase beta family with a crotonase-like fold; together with MdcE, it generates the oxyanion-stabilized active site at the subunit interface. (Hoenke et al. 1997; Maderbocus et al. 2017) (hoenke1997sequenceofa pages 4-5, maderbocus2017crystalstructureof pages 2-4)
- Specialized acyl carrier protein (MdcC): A small ACP bearing 2′-(5″-phosphoribosyl)-3′-dephospho-CoA attached via a conserved serine (e.g., Ser25), distinct from fatty-acid ACPs; it shuttles acetyl and malonyl groups between MdcA and MdcD–MdcE active sites. (Hoenke et al. 1997; Chohnan & Takamura 2004; Maderbocus et al. 2017) (hoenke1997sequenceofa pages 1-2, chohnan2004malonatedecarboxylasein pages 2-4, maderbocus2017crystalstructureof pages 1-2)

2) Recent developments and latest research (emphasis 2017–present)
- High-resolution structures of the MdcD–MdcE carboxyltransferase and the full MdcA–MdcC–MdcD–MdcE hetero-tetramer revealed: (i) MdcD and MdcE are crotonase-fold proteins; (ii) the active site lies at the D/E interface and contains a conserved oxyanion hole; (iii) malonate binds to MdcA, while CoA can bind at the D/E site in structural mimics; (iv) subunit interfaces are essential for holoenzyme assembly and bacterial growth on malonate; (v) the catalytic centers of MdcA and MdcD/E are ~60 Å apart, implying conformational dynamics or alternative assembly states during catalysis. Mutations in interface or active-site residues abolished growth on malonate in Pseudomonas, directly linking structure to physiological function. (Maderbocus et al. 2017, Nature Communications, 2017-07-18, https://doi.org/10.1038/s41467-017-00233-z) (maderbocus2017crystalstructureof pages 1-2, maderbocus2017crystalstructureof pages 2-4, maderbocus2017crystalstructureof pages 10-10)
- Substrate scope observations: While the physiological substrate for MdcD–MdcE is malonyl-S-ACP, Pseudomonas MdcD–MdcE shows weak malonyl-CoA decarboxylase activity in vitro, far lower than human MCD, suggesting limited catalytic promiscuity and reinforcing that ACP tethering is central in vivo. (Maderbocus et al. 2017) (maderbocus2017crystalstructureof pages 10-10)
- Note on literature landscape: Within the retrieved evidence set, post-2017 primary advances on MDC structure/function center on the Nature Communications work; additional 2023–2024 organism-specific or AM1 studies were not retrieved here and thus are not cited. We flag this as a limitation and encourage targeted genome context searches for AM1 in specialized databases.

3) Current applications and real-world implementations
- Metabolic and physiological role: MDC enables bacterial growth on malonate as sole carbon/energy source; expression of mdc operons in heterologous hosts confers malonate utilization, demonstrating biotechnological portability of the pathway. (Hoenke et al. 1997, expression in E. coli; Dimroth & Hilbi 1997) (hoenke1997sequenceofa pages 1-2, dimroth1997enzymicandgenetic pages 4-6)
- Analytical application: The enzyme system has been used to determine intracellular acyl-CoA thioesters, leveraging the specificity of malonyl-ACP decarboxylation and associated reactions. (Chohnan & Takamura 2004, Microbes Environ, 2004-09, https://doi.org/10.1264/jsme2.19.179) (chohnan2004malonatedecarboxylasein pages 2-4)
- Antibacterial target rationale: Structural mutagenesis that disrupts MDC assembly eliminates growth on malonate in Pseudomonas, suggesting MDC as a potential niche-specific target where malonate utilization contributes to fitness; the holoenzyme’s defined interfaces provide tractable sites. (Maderbocus et al. 2017) (maderbocus2017crystalstructureof pages 1-2, maderbocus2017crystalstructureof pages 2-4)

4) Expert opinions and analysis from authoritative sources
- Operon architecture and evolutionary conservation: Foundational reviews and operon sequencing demonstrate conserved core genes (mdcA/C/D/E with ACP prosthetic-function genes and transport/regulation). The biotin-independent MDC is soluble/cytosolic and relies on the specialized ACP rather than a tethered biotin cofactor, mechanistically paralleling but distinct from classical biotin-dependent carboxylases. (Dimroth & Hilbi 1997; Hoenke et al. 1997; Chohnan & Takamura 2004) (dimroth1997enzymicandgenetic pages 4-6, hoenke1997sequenceofa pages 1-2, chohnan2004malonatedecarboxylasein pages 2-4)
- Structural mechanism: High-resolution structures argue for an oxyanion-stabilized decarboxylation at the MdcD/E interface, with dynamics to bring ACP-tethered intermediates between MdcA and MdcD/E active sites; the crotonase-like architecture underpins the carboxyltransferase chemistry. (Maderbocus et al. 2017) (maderbocus2017crystalstructureof pages 2-4, maderbocus2017crystalstructureof pages 10-10)

5) Relevant statistics and data from recent studies
- Subunit composition: Hetero-tetramer stoichiometry MdcA:MdcC:MdcD:MdcE = 1:1:1:1 in Pseudomonas; oligomeric behavior of D/E varies by species (heterodimer in solution vs. heterotetramer reported historically), but active site is consistently at the D/E interface. (Maderbocus et al. 2017) (maderbocus2017crystalstructureof pages 1-2, maderbocus2017crystalstructureof pages 2-4)
- Kinetic specificity: MdcD–MdcE can decarboxylate malonyl-CoA weakly in vitro; catalytic efficiency is ~38-fold lower (kcat/Km) than human malonyl-CoA decarboxylase, highlighting that the natural substrate is malonyl-ACP. (Maderbocus et al. 2017) (maderbocus2017crystalstructureof pages 10-10)
- Genetic organization: Klebsiella mdc cluster comprises eight to nine contiguous genes (mdcABCDEFCH with divergently transcribed mdcR); expression in E. coli confers activity, and MdcF is the sole hydrophobic (putative transporter) component in that cluster. (Hoenke et al. 1997, 1997-06, https://doi.org/10.1111/j.1432-1033.1997.00530.x) (hoenke1997sequenceofa pages 1-2)

Functional annotation for Methylorubrum extorquens AM1 mdcD (UniProt C5APL4; locus META1p0025)
- Primary function and catalytic activity: mdcD encodes the beta subunit of the malonate decarboxylase carboxyltransferase (MdcD–MdcE). The physiological reaction performed by the MdcD–MdcE pair is decarboxylation of malonyl-S-ACP to form acetyl-S-ACP and CO2, consuming a proton; this step regenerates acetyl-ACP in the MDC cycle. Substrate specificity is for ACP-tethered malonyl intermediates produced by MdcA/MdcH; malonyl-CoA can be a poor in vitro substrate in some systems but is not the native substrate. (Hoenke et al. 1997; Chohnan & Takamura 2004; Maderbocus et al. 2017) (hoenke1997sequenceofa pages 1-2, chohnan2004malonatedecarboxylasein pages 2-4, maderbocus2017crystalstructureof pages 10-10)
- Role within the complex: MdcD forms a heteromer with MdcE to generate the carboxyltransferase active site; together they interact with MdcC (ACP) to receive malonyl-ACP for decarboxylation. Structural data locate the active site at the D/E interface with a crotonase-like fold and conserved oxyanion hole. (Maderbocus et al. 2017) (maderbocus2017crystalstructureof pages 2-4)
- Cellular localization: The biotin-independent MDC (including MdcD) is a soluble, cytosolic complex. Associated operons often encode a membrane transporter (e.g., MdcF) for malonate uptake, but the decarboxylase core (MdcA/C/D/E/H) is cytosolic. (Dimroth & Hilbi 1997; Hoenke et al. 1997; Chohnan & Takamura 2004) (dimroth1997enzymicandgenetic pages 4-6, hoenke1997sequenceofa pages 1-2, chohnan2004malonatedecarboxylasein pages 2-4)
- Pathway context: MDC enables malonate catabolism. The cycle begins with MdcA catalyzing acetyl-ACP:malonate transfer to generate malonyl-ACP (with initiation aided by MdcH), followed by MdcD–MdcE decarboxylation to regenerate acetyl-ACP. The ACP prosthetic group is unique (2′-(5″-phosphoribosyl)-3′-dephospho-CoA on Ser25), and accessory enzymes (MdcB/G) assemble this moiety. The overall pathway bypasses biotin and differs mechanistically from biotin-dependent carboxylases. (Hoenke et al. 1997; Chohnan & Takamura 2004; Dimroth & Hilbi 1997; Maderbocus et al. 2017) (hoenke1997sequenceofa pages 1-2, chohnan2004malonatedecarboxylasein pages 2-4, dimroth1997enzymicandgenetic pages 4-6, maderbocus2017crystalstructureof pages 1-2)
- Gene/operon organization and conservation: Across bacteria, mdc genes are tightly clustered with short intergenic regions, typically including mdcA/C/D/E, the ACP prosthetic-group genes (e.g., mdcB/G), a malonate transporter (mdcF), an ancillary transacylase (mdcH), and a LysR-type regulator (mdcR). This organization underlies coordinated expression and function, and heterologous expression confers malonate utilization. (Hoenke et al. 1997; Dimroth & Hilbi 1997; Chohnan & Takamura 2004) (hoenke1997sequenceofa pages 1-2, dimroth1997enzymicandgenetic pages 4-6, chohnan2004malonatedecarboxylasein pages 2-4)

Organism-specific notes for M. extorquens AM1
- Verification and ambiguity: The symbol mdcD can be used in many bacteria for the MDC beta subunit. No conflicting gene/protein with the same symbol in M. extorquens AM1 was found in the retrieved evidence. The UniProt accession C5APL4 and locus META1p0025 identify the AM1 protein as an MDC beta subunit, and its predicted domains (AcCoA_carboxylase_beta; crotonase-like; COA_CT_N; PF01039) are fully consistent with the MDC D/E carboxyltransferase family described above, supporting functional inference by homology. Direct AM1-specific experimental data (genetics/biochemistry of mdcD at META1p0025) were not retrieved in this search and therefore are not cited here; conclusions for AM1 are inferred from conserved function across mdcD orthologs. (Dimroth & Hilbi 1997; Hoenke et al. 1997; Chohnan & Takamura 2004; Maderbocus et al. 2017) (dimroth1997enzymicandgenetic pages 4-6, hoenke1997sequenceofa pages 1-2, chohnan2004malonatedecarboxylasein pages 2-4, maderbocus2017crystalstructureof pages 1-2)

Limitations and recommendations
- 2023–2024 primary AM1-specific publications were not retrieved in this search scope. If AM1 genome context or expression evidence is required, we recommend targeted genome database queries (RefSeq/ENA) for META1p0025 synteny and RNA-seq datasets, and literature searches focused on “Methylorubrum extorquens AM1 malonate decarboxylase mdc operon.”

Cited sources (URLs and dates)
- Dimroth P, Hilbi H. Enzymic and genetic basis for bacterial growth on malonate. Molecular Microbiology. 1997-07. https://doi.org/10.1046/j.1365-2958.1997.4611824.x (dimroth1997enzymicandgenetic pages 4-6)
- Hoenke S, Schmid M, Dimroth P. Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli. European Journal of Biochemistry. 1997-06. https://doi.org/10.1111/j.1432-1033.1997.00530.x (hoenke1997sequenceofa pages 1-2, hoenke1997sequenceofa pages 4-5)
- Chohnan S, Takamura Y. Malonate Decarboxylase in Bacteria and Its Application for Determination of Intracellular Acyl-CoA Thioesters. Microbes and Environments. 2004-09. https://doi.org/10.1264/jsme2.19.179 (chohnan2004malonatedecarboxylasein pages 2-4)
- Maderbocus R, Fields BL, Hamilton K, et al. Crystal structure of a Pseudomonas malonate decarboxylase holoenzyme hetero-tetramer. Nature Communications. 2017-07-18. https://doi.org/10.1038/s41467-017-00233-z (maderbocus2017crystalstructureof pages 1-2, maderbocus2017crystalstructureof pages 2-4, maderbocus2017crystalstructureof pages 10-10)

References

1. (hoenke1997sequenceofa pages 1-2): Stefan Hoenke, Markus Schmid, and Peter Dimroth. 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, Jun 1997. URL: https://doi.org/10.1111/j.1432-1033.1997.00530.x, doi:10.1111/j.1432-1033.1997.00530.x. This article has 53 citations.

2. (hoenke1997sequenceofa pages 4-5): Stefan Hoenke, Markus Schmid, and Peter Dimroth. 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, Jun 1997. URL: https://doi.org/10.1111/j.1432-1033.1997.00530.x, doi:10.1111/j.1432-1033.1997.00530.x. This article has 53 citations.

3. (maderbocus2017crystalstructureof pages 1-2): Riyaz Maderbocus, Blanche L. Fields, Keith Hamilton, Shukun Luo, Timothy H. Tran, Lars E. P. Dietrich, and Liang Tong. Crystal structure of a pseudomonas malonate decarboxylase holoenzyme hetero-tetramer. Nature Communications, Jul 2017. URL: https://doi.org/10.1038/s41467-017-00233-z, doi:10.1038/s41467-017-00233-z. This article has 19 citations and is from a highest quality peer-reviewed journal.

4. (maderbocus2017crystalstructureof pages 2-4): Riyaz Maderbocus, Blanche L. Fields, Keith Hamilton, Shukun Luo, Timothy H. Tran, Lars E. P. Dietrich, and Liang Tong. Crystal structure of a pseudomonas malonate decarboxylase holoenzyme hetero-tetramer. Nature Communications, Jul 2017. URL: https://doi.org/10.1038/s41467-017-00233-z, doi:10.1038/s41467-017-00233-z. This article has 19 citations and is from a highest quality peer-reviewed journal.

5. (dimroth1997enzymicandgenetic pages 4-6): Peter Dimroth and Hubert Hilbi. Enzymic and genetic basis for bacterial growth on malonate. Molecular Microbiology, 25:3-10, Jul 1997. URL: https://doi.org/10.1046/j.1365-2958.1997.4611824.x, doi:10.1046/j.1365-2958.1997.4611824.x. This article has 66 citations and is from a domain leading peer-reviewed journal.

6. (chohnan2004malonatedecarboxylasein pages 2-4): Shigeru Chohnan and Yoshichika Takamura. Malonate decarboxylase in bacteria and its application for determination of intracellular acyl-coa thioesters. Microbes and Environments, 19:179-189, Sep 2004. URL: https://doi.org/10.1264/jsme2.19.179, doi:10.1264/jsme2.19.179. This article has 16 citations and is from a peer-reviewed journal.

7. (maderbocus2017crystalstructureof pages 10-10): Riyaz Maderbocus, Blanche L. Fields, Keith Hamilton, Shukun Luo, Timothy H. Tran, Lars E. P. Dietrich, and Liang Tong. Crystal structure of a pseudomonas malonate decarboxylase holoenzyme hetero-tetramer. Nature Communications, Jul 2017. URL: https://doi.org/10.1038/s41467-017-00233-z, doi:10.1038/s41467-017-00233-z. This article has 19 citations and is from a highest quality peer-reviewed journal.

Citations

1. maderbocus2017crystalstructureof pages 10-10
2. chohnan2004malonatedecarboxylasein pages 2-4
3. hoenke1997sequenceofa pages 1-2
4. maderbocus2017crystalstructureof pages 2-4
5. dimroth1997enzymicandgenetic pages 4-6
6. hoenke1997sequenceofa pages 4-5
7. maderbocus2017crystalstructureof pages 1-2
8. https://doi.org/10.1038/s41467-017-00233-z
9. https://doi.org/10.1264/jsme2.19.179
10. https://doi.org/10.1111/j.1432-1033.1997.00530.x
11. https://doi.org/10.1046/j.1365-2958.1997.4611824.x
12. https://doi.org/10.1111/j.1432-1033.1997.00530.x,
13. https://doi.org/10.1038/s41467-017-00233-z,
14. https://doi.org/10.1046/j.1365-2958.1997.4611824.x,
15. https://doi.org/10.1264/jsme2.19.179,