Mabinlin 2
| Mabinlin 2 | ||
|---|---|---|
| nach PDB 2DS2 | ||
| Andere Namen |
Mabinlin II, MAB II, Sweet protein mabinlin-2 | |
| Präkursor | 155 Aminosäuren, 18.089 Da | |
| Bezeichner | ||
| Externe IDs | ||
Mabinlin 2 ist ein Protein aus der chinesischen Pflanze Capparis masaikai (Mabinlang), das einen Süßgeschmack auf der Zunge von Menschen erzeugt.
Eigenschaften
Mabinlin 2 gehört, wie auch seine Homologe Mabinlin 1, Mabinlin 3 und Mabinlin 4, zu den 2S-Speicherproteinen von Mabinlang.[1] Es besitzt vier Disulfidbrücken und ist thermostabil.[1] Unter den Mabinlinen besitzt Mabinlin 2 die höchste Thermostabilität.[2] Nach der Translation wird es posttranslational durch Proteolyse in zwei Teile gespalten, Kette A (Position 36–68) und Kette B (Position 83–154).[1] An den Positionen 36 und 83 befindet sich eine Pyrrolidoncarbonsäure.[1]
Homologe von Mabinlin 2
Kette A
M-1: EPLCRRQFQQ HQHLRACQRY IRRRAQRGGL VD
M-2: QLWRCQRQFL QHQRLRACQR FIHRRAQFGG QPD
M-3: EPLCRRQFQQ HQHLRACQRY LRRRAQRGGL AD
M-4: EPLCRRQFQQ HQHLRACQRY LRRRAQRG
Kette B
M-1: EQRGPALRLC CNQLRQVNKP CVCPVLRQAA HQQLYQGQIE GPRQVRQLFR AARNLPNICK IPAVGRCQFT RW
M-2: QPRRPALRQC CNQLRQVDRP CVCPVLRQAA QQVLQRQIIQ GPQQLRRLFD AARNLPNICN IPNIGACPFR AW
M-3: EQRGPALRLC CNQLRQVNKP CVCPVLRQAA HQQLYQGQIE GPRQVRRLFR AARNLPNICK IPAVGRCQFT RW
M-4: EQRGPALRLC CNQLRQVNKP CVCPVLRQAA HQQLYQGQIE GPRQVRRLFR AARNLPNICK IPAVGRCQFT RW
Aminosäuresequenzen nach UniProt.[3][4][5][6]
Literatur
- X. Liu, S. Maeda, Z. Hu, T. Aiuchi, K. Nakaya, Y. Kurihara: Purification, complete amino acid sequence and structural characterization of the heat-stable sweet protein, mabinlin II. In: European Journal of Biochemistry. Band 211, Nummer 1–2, Januar 1993, S. 281–287, PMID 8425538.
- Z. Hu, M. He: Studies on mabinlin, a sweet protein from the seeds of Capparis masaikai levl. I. extraction, purification and certain characteristics. In: Acta Botan. Yunnan. (1983), Band 5, S. 207–212.
- S. Nirasawa, T. Nishino, M. Katahira, S. Uesugi, Z. Hu, Y. Kurihara: Structures of heat-stable and unstable homologues of the sweet protein mabinlin. The difference in the heat stability is due to replacement of a single amino acid residue. In: European Journal of Biochemistry. Band 223, Nummer 3, August 1994, S. 989–995, PMID 8055976.
- Y. Kurihara: Characteristics of antisweet substances, sweet proteins, and sweetness-inducing proteins. In: Critical reviews in food science and nutrition. Band 32, Nummer 3, 1992, S. 231–252, doi:10.1080/10408399209527598, PMID 1418601.
Einzelnachweise
- ↑ a b c d UniProt Sweet protein mabinlin-2 precursor - Capparis masaikai (Mabinlang). Abgerufen am 24. Oktober 2018.
- ↑ R. J. Guan, J. M. Zheng, Z. Hu, D. C. Wang: Crystallization and preliminary X-ray analysis of the thermostable sweet protein mabinlin II. In: Acta crystallographica. Section D, Biological crystallography. Band 56, Pt 7Juli 2000, S. 918–919, PMID 10930844.
- ↑ UniProt P80351
- ↑ UniProt P30233
- ↑ UniProt P80352
- ↑ UniProt P80353
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