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Comprehensive Structural Characterization of the Bacterial Homospermidine Synthase–an Essential Enzyme of the Polyamine Metabolism

https://doi.org/10.1038/srep19501

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?

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Mammalian polyamine metabolism and function

inferredcites →https://doi.org/10.1006/abio.1997.2091openalex-snapshot

High-Resolution Reversed-Phase High-Performance Liquid Chromatography Analysis of Polyamines and Their Monoacetyl Conjugates by Fluorescence Detection after Derivatization withN-Hydroxysuccinimidyl 6-Quinolinyl Carbamate

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Conformational Flexibility in Glutamate Dehydrogenase

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Current Status of the Polyamine Research Field

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Molecular Evolution by Change of Function

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PDBsum additions

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XDS

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Different polyamine pathways from bacteria have replaced eukaryotic spermidine biosynthesis in ciliates T etrahymena thermophila and P aramecium tetaurelia

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Crystal Structure of the His-Tagged Saccharopine Reductase From Saccharomyces cerevisiae at 1.7-Å Resolution

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Homospermidine synthase of Rhodopseudomonas viridis: Substrate specificity and effects of the heterologously expressed enzyme on polyamine metabolism of Escherichia coli.

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Rational Engineering of Homospermidine Synthase for Enhanced Catalytic Efficiency Toward Spermidine Synthesis

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Microbial Engineering for Production of N‐Functionalized Amino Acids and Amines

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Unusual Polyamines from Baikalian Diatoms

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Kinetic and structural characterization of carboxyspermidine dehydrogenase of polyamine biosynthesis

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Mutually exclusive pathways for biosynthesis of polyamine homospermidine dependent on putrescine or agmatine

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Rational engineering of homospermidine synthase for enhanced catalytic efficiency toward spermidine synthesis

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Insights into the Unusual Activity of a Novel Homospermidine Synthase with a Promising Application to Produce Spermidine

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inferred← citeshttps://doi.org/10.1038/s41598-020-69401-4openalex-snapshot

Gene products and processes contributing to lanthanide homeostasis and methanol metabolism in Methylorubrum extorquens AM1

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Caldomycin, a new guanidopolyamine produced by a novel agmatine homocoupling enzyme involved in homospermidine biosynthesis

inferred← citeshttps://doi.org/10.1042/bcj20160185openalex-snapshot

Biosynthesis of polyamines and polyamine-containing molecules

inferred← citeshttps://doi.org/10.1042/bcj20160823openalex-snapshot

Evolution of biosynthetic diversity

inferred← citeshttps://doi.org/10.1073/pnas.2214165120openalex-snapshot

Functional polyamine metabolic enzymes and pathways encoded by the virosphere

inferred← citeshttps://doi.org/10.1080/07391102.2018.1475260openalex-snapshot

Human p38α mitogen-activated protein kinase in the Asp168-Phe169-Gly170-in (DFG-in) state can bind allosteric inhibitor Doramapimod

inferred← citeshttps://doi.org/10.1093/femsle/fnz084openalex-snapshot

Polyamine biosynthesis and biological roles in rhizobia

inferred← citeshttps://doi.org/10.1099/mic.0.001668openalex-snapshot

Divergent and overlapping roles of homospermidine and spermidine in Sinorhizobium meliloti physiology and symbiotic performance

inferred← citeshttps://doi.org/10.1101/647677openalex-snapshot

Lanthanide transport, storage, and beyond: gene products and processes contributing to lanthanide and methanol metabolism in Methylorubrum extorquens AM1

inferred← citeshttps://doi.org/10.1107/s2059798321008937openalex-snapshot

Structural and catalytic characterization of Blastochloris viridis and Pseudomonas aeruginosa homospermidine synthases supports the essential role of cation–π interaction

inferred← citeshttps://doi.org/10.1111/febs.14486openalex-snapshot

Neuraminidase A from Streptococcus pneumoniae has a modular organization of catalytic and lectin domains separated by a flexible linker

inferred← citeshttps://doi.org/10.1128/mbio.01091-21openalex-snapshot

SAR11 Cells Rely on Enzyme Multifunctionality To Metabolize a Range of Polyamine Compounds

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Exploration expérimentale du métabolisme du soufre dans le vivant

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