Biology:BpsA
| N4-bis(aminopropyl)spermidine synthase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 2.5.1.128 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
BpsA (N(4)-bis(aminopropyl)spermidine synthase) is a single-module non-ribosomal peptide synthase (NRPS) (also see non-ribosomal peptide (NPR)) located in the cytoplasm[1] responsible for the process of creating branched-chain polyamines,[1] and producing spermidine and spermine.[2] It has a singular ligand in its structure involved with Fe3+ and PLIP interactions.[3] As seen by its EC number, it is a transferase (2) that transfers an alkyl or aryl group other than methyl groups (5) (2.5.1).[citation needed] BpsA was first discovered in the archaea Methanococcus jannaschii[4] and thermophile Thermococcus kodakarensis [2] and since then has been used in a variety of applications such as being used as a reporter, researching phosphopantetheinyl transferase (PPTase), and for NRPS domain recombination experiments it can be used as a model.[5] Both (hyper)thermophilic bacteria and euryarchaeotal archaea seem to conserve BpsA and orthologs as branches chains polyamines are crucial for survival.[6] There is also a second type of BpsA also known as Blue-pigment indigoidine synthetase that produces the pigment indigoidine and is found in organisms like Erwinia chrysanthemi.[7] However, not much seems to be known about this variant except that it is a synthase, and it does not yet appear to be classified under an EC number.
Thermophiles
In thermophiles, BpsA converts N4-aminopropylspermidine to N4-bis(aminopropyl)spermidine.[2] In this pathway, aminopropyltransferase and ureohydrolase turn N1-aminopropylagmatine to agmantine and synthesize spermidine and spermine.[2] Spermine and spermadine are utilized in a variety of pathways including macromolecule production, apoptosis and proliferation equilibrium, and the induction of differentiation in cells.[8] Long Linear polyamines (such as ones found in TK-BpsA made of up spermine and spermidine) help stabilize DNA.[8] Denaturation could possible occur at high temperatures, making the stabilization crucial for organisms that thrive here. If an organism cannot stabilize its DNA, it cannot survive. TK-BpsA is a BpsA found in the archaeon Thermococcus kodakarensis and is used to study this pathway more in depth.[9] It is also a ternary complex.[10] There are a few active sites that include polyamine spermidine/spermine synthases, and loop-closures occur upon the binding of spermidine, and a catalytic center made of a Gly-Asp-Asp-Asp motif which contains reactive secondary amino group of the substrate polyamine and a sulfur atom of the product 5ʹ-methylthioadenosine with Asp 159.[9] The enzyme proves itself to be important to thermophiles as it supports growth under high-temperature conditions.[1] In this system, the C-Terminal is a flexible region of branched-chain polyamine synthase facilitates substrate specificity and catalysis.[10] This C-terminal region recognizes acceptor proteins for the enzyme and gain their flexibility from aspartate/glutamate residues.[10] The flexibility itself is promoted by a ping-pong Bi-Bi mechanism that occurs when temperatures are high.[10]
References
- ↑ 1.0 1.1 1.2 "Q58669 · BPSA_METJA". UniProt. https://www.uniprot.org/uniprotkb/Q58669/entry#family_and_domains.
- ↑ 2.0 2.1 2.2 2.3 "Identification of a novel aminopropyltransferase involved in the synthesis of branched-chain polyamines in hyperthermophiles". Journal of Bacteriology 196 (10): 1866–1876. May 2014. doi:10.1128/JB.01515-14. PMID 24610711.
- ↑ "Q58669 (BPSA_METJA)". SWISS-MODEL Repository. https://swissmodel.expasy.org/repository/md5/6af45151b678865cd36debb6ef9e7335?template=2qm3.
- ↑ "Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii". Science 273 (5278): 1058–1073. August 1996. doi:10.1126/science.273.5278.1058. PMID 8688087. Bibcode: 1996Sci...273.1058B.
- ↑ "A sensitive single-enzyme assay system using the non-ribosomal peptide synthetase BpsA for measurement of L-glutamine in biological samples". Scientific Reports 7 (1): 41745. January 2017. doi:10.1038/srep41745. PMID 28139746. Bibcode: 2017NatSR...741745B.
- ↑ "Identification of Branched-Chain Polyamines in Hyperthermophiles". Polyamines. Methods in Molecular Biology. 1694. New York, NY: Springer. 2018. pp. 81–94. doi:10.1007/978-1-4939-7398-9_8. ISBN 978-1-4939-7398-9.
- ↑ "Characterization of indigoidine biosynthetic genes in Erwinia chrysanthemi and role of this blue pigment in pathogenicity". Journal of Bacteriology 184 (3): 654–665. February 2002. doi:10.1128/JB.184.3.654-665.2002. PMID 11790734.
- ↑ 8.0 8.1 "Stabilization of nucleic acids by unusual polyamines produced by an extreme thermophile, Thermus thermophilus". The Biochemical Journal 388 (Pt 2): 427–433. June 2005. doi:10.1042/BJ20041778. PMID 15673283.
- ↑ 9.0 9.1 "Active site geometry of a novel aminopropyltransferase for biosynthesis of hyperthermophile-specific branched-chain polyamine". The FEBS Journal 284 (21): 3684–3701. November 2017. doi:10.1111/febs.14262. PMID 28881427.
- ↑ 10.0 10.1 10.2 10.3 "The C-terminal flexible region of branched-chain polyamine synthase facilitates substrate specificity and catalysis". The FEBS Journal 286 (19): 3926–3940. October 2019. doi:10.1111/febs.14949. PMID 31162806.
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