Ser-His
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| Category | Others |
| Catalog number | BBF-05531 |
| CAS | 67726-09-4 |
| Molecular Weight | 242.23 |
| Molecular Formula | C9H14N4O4 |
| Purity | ≥95% |
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Description
Seryl-histidine is a dipeptide composed of serine and histidine. It is an incomplete breakdown product of protein digestion or protein catabolism.
Specification
| Synonyms | serylhistidine; L-seryl-L-histidine; L-Histidine, N-L-seryl-; SH dipeptide; L-Ser-L-His; Serine Histidine dipeptide; (S)-2-((S)-2-Amino-3-hydroxypropanamido)-3-(1H-imidazol-4-yl)propanoic acid |
| Sequence | H-Ser-His-OH |
| Storage | Store at -20°C |
| IUPAC Name | (2S)-2-[[(2S)-2-amino-3-hydroxypropanoyl]amino]-3-(1H-imidazol-5-yl)propanoic acid |
| Canonical SMILES | C1=C(NC=N1)CC(C(=O)O)NC(=O)C(CO)N |
| InChI | InChI=1S/C9H14N4O4/c10-6(3-14)8(15)13-7(9(16)17)1-5-2-11-4-12-5/h2,4,6-7,14H,1,3,10H2,(H,11,12)(H,13,15)(H,16,17)/t6-,7-/m0/s1 |
| InChI Key | YZMPDHTZJJCGEI-BQBZGAKWSA-N |
Properties
| Appearance | Solid |
| Boiling Point | 763.4±60.0°C at 760 mmHg |
| Density | 1.5±0.1 g/cm3 |
| Solubility | Soluble in DMSO, Water |
Reference Reading
1. Selective Formation of Ser-His Dipeptide via Phosphorus Activation
Wanyun Shu, Yongfei Yu, Su Chen, Xia Yan, Yan Liu, Yufen Zhao Orig Life Evol Biosph. 2018 Jun;48(2):213-222. doi: 10.1007/s11084-018-9556-7. Epub 2018 Apr 29.
The Ser-His dipeptide is the shortest active peptide. This dipeptide not only hydrolyzes proteins and DNA but also catalyzes the formation of peptides and phosphodiester bonds. As a potential candidate for the prototype of modern hydrolase, Ser-His has attracted increasing attention. To explore if Ser-His could be obtained efficiently in the prebiotic condition, we investigated the reactions of N-DIPP-Ser with His or other amino acids in an aqueous system. We observed that N-DIPP-Ser incubated with His can form Ser-His more efficiently than with other amino acids. A synergistic effect involving the two side chains of Ser and His is presumed to be the critical factor for the selectivity of this specific peptide formation.
2. Structural analysis of a Vibrio phospholipase reveals an unusual Ser-His-chloride catalytic triad
Ye Wan, Changshui Liu, Qingjun Ma J Biol Chem. 2019 Jul 26;294(30):11391-11401. doi: 10.1074/jbc.RA119.008280. Epub 2019 May 9.
Phospholipases can disrupt host membranes and are important virulence factors in many pathogens. VvPlpA is a phospholipase A2 secreted by Vibrio vulnificus and essential for virulence. Its homologs, termed thermolabile hemolysins (TLHs), are widely distributed in Vibrio bacteria, but no structural information for this virulence factor class is available. Herein, we report the crystal structure of VvPlpA to 1.4-Å resolution, revealing that VvPlpA contains an N-terminal domain of unknown function and a C-terminal phospholipase domain and that these two domains are packed closely together. The phospholipase domain adopts a typical SGNH hydrolase fold, containing the four conserved catalytic residues Ser, Gly, Asn, and His. Interestingly, the structure also disclosed that the phospholipase domain accommodates a chloride ion near the catalytic His residue. The chloride is five-coordinated in a distorted bipyramid geometry, accepting hydrogen bonds from a water molecule and the amino groups of surrounding residues. This chloride substitutes for the most common Asp/Glu residue and forms an unusual Ser-His-chloride catalytic triad in VvPlpA. The chloride may orient the catalytic His and stabilize the charge on its imidazole ring during catalysis. Indeed, VvPlpA activity depended on chloride concentration, confirming the important role of chloride in catalysis. The VvPlpA structure also revealed a large hydrophobic substrate-binding pocket that is capable of accommodating a long-chain acyl group. Our results provide the first structure of the TLH family and uncover an unusual Ser-His-chloride catalytic triad, expanding our knowledge on the biological role of chloride.
3. Structural insight into molecular mechanism of poly(ethylene terephthalate) degradation
Seongjoon Joo, In Jin Cho, Hogyun Seo, Hyeoncheol Francis Son, Hye-Young Sagong, Tae Joo Shin, So Young Choi, Sang Yup Lee, Kyung-Jin Kim Nat Commun. 2018 Jan 26;9(1):382. doi: 10.1038/s41467-018-02881-1.
Plastics, including poly(ethylene terephthalate) (PET), possess many desirable characteristics and thus are widely used in daily life. However, non-biodegradability, once thought to be an advantage offered by plastics, is causing major environmental problem. Recently, a PET-degrading bacterium, Ideonella sakaiensis, was identified and suggested for possible use in degradation and/or recycling of PET. However, the molecular mechanism of PET degradation is not known. Here we report the crystal structure of I. sakaiensis PETase (IsPETase) at 1.5 Å resolution. IsPETase has a Ser-His-Asp catalytic triad at its active site and contains an optimal substrate binding site to accommodate four monohydroxyethyl terephthalate (MHET) moieties of PET. Based on structural and site-directed mutagenesis experiments, the detailed process of PET degradation into MHET, terephthalic acid, and ethylene glycol is suggested. Moreover, other PETase candidates potentially having high PET-degrading activities are suggested based on phylogenetic tree analysis of 69 PETase-like proteins.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
