Ornithine carbamoyltransferase from psychrophiles to thermophiles : structural evolution of catalytic fold to accommodate physiological diversity
Here, we have analyzed the enzyme ornithine carbamoyltransferase (OCTase) in different classes of microorganisms belonging to psychrophiles, mesophiles and thermophiles. This OCTase catalyzes the formation of citrulline from carbamoyl phosphate (CP) and ornithine (ORN) in arginine biosynthesis pathway and has certain unique adaptations to regulate metabolic pathways in extreme conditions. The tertiary structure of OCTase showed two binding domains, the CP domain and ORN-binding domain at N and C terminals, respectively. We propose general acid-base catalysis in Pseudomonas gessardii between His259 and Asp220 in which later may act as a recipient of proton in the process. The comparative docking analysis showed that substrate-binding loops have been evolved to accommodate their lifestyles across the physiological temperature range where two substrates bind on two distinct loops in psychrophiles and mesophiles, whereas both the substrates bind on a single-substrate-binding loop in thermophiles and bring down the flexibility of the active site pocket to improve its evolutionary fitness.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:25 |
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| Enthalten in: |
Extremophiles : life under extreme conditions - 25(2021), 1 vom: 21. Jan., Seite 15-24 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Sharma, Shivika [VerfasserIn] |
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| Links: |
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| Themen: |
590-55-6 |
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| Anmerkungen: |
Date Completed 09.02.2021 Date Revised 09.02.2021 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1007/s00792-020-01208-7 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM316541737 |
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| 245 | 1 | 0 | |a Ornithine carbamoyltransferase from psychrophiles to thermophiles |b structural evolution of catalytic fold to accommodate physiological diversity |
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| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Here, we have analyzed the enzyme ornithine carbamoyltransferase (OCTase) in different classes of microorganisms belonging to psychrophiles, mesophiles and thermophiles. This OCTase catalyzes the formation of citrulline from carbamoyl phosphate (CP) and ornithine (ORN) in arginine biosynthesis pathway and has certain unique adaptations to regulate metabolic pathways in extreme conditions. The tertiary structure of OCTase showed two binding domains, the CP domain and ORN-binding domain at N and C terminals, respectively. We propose general acid-base catalysis in Pseudomonas gessardii between His259 and Asp220 in which later may act as a recipient of proton in the process. The comparative docking analysis showed that substrate-binding loops have been evolved to accommodate their lifestyles across the physiological temperature range where two substrates bind on two distinct loops in psychrophiles and mesophiles, whereas both the substrates bind on a single-substrate-binding loop in thermophiles and bring down the flexibility of the active site pocket to improve its evolutionary fitness | ||
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| 650 | 4 | |a Extremophiles | |
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| 650 | 4 | |a Ornithine carbamoyltransferase | |
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| 700 | 1 | |a Ahmed, Mushtaq |e verfasserin |4 aut | |
| 700 | 1 | |a Akhter, Yusuf |e verfasserin |4 aut | |
| 700 | 1 | |a Chatterjee, Subhankar |e verfasserin |4 aut | |
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