Amino acid sequence and secondary structural analysis of the corn inhibitor of trypsin and activated Hageman Factor.

A novel strategy for inhibition of α-amylases: yellow meal worm α-amylase in complex with the Ragi bifunctional inhibitor at 2.5 å resolution

“…This figure was made with MOLMOL [39]. SAGT-SCVPGWAIPHNPLPSCRWYVTSRTCGI----GPRLPW---PEL-KRRCCRELADIPA-YCRCTAL [42] Rye TI (62 %) SVGG-QCVPGLAMPHNPLGACRTYVVSQICHV----GPRLFT---WDM-KRRCCDELLAIPA-YCRCEAL [43] Barley TI/CMe (56 %) (S)FGD-SCAPGDALPHNPLRACRTYVVSQICHQ----GPRLLT---SDM-KRRCCDELSAIPA-YCRCEAL α-Amylase inhibitors active as monomers or homodimers [44] Sorghum AI SIalpha4 (43 %) TVDVTACAPGLAIPAPPLPTCRTFARPRTCGLGGPYGPVDPS---PVL-KQRCCRELAAVPS-RCRCAAL [44] Sorghum AI SIalpha5 (41 %) ANW--CEPGLVIPLNPLPSCRTYMVRRACGVSI--GPVVPL---PVL-KERCCSELEKLVP-YCRCGAL [45] Barley CMa (41 %) TGQY--CYAGMGLPSNPLEGCREYVAQQTCGVTIA-GSPVSSEPGDTP-KDRCCQELDEAPQ-HCRCEAV [46] Wheat AI 0.19 (26 %) SGPW-MCYPGQAFQVPALPACRPLLRLQ-CN-----GSQV-----PEAVLRDCCQQLAHISE-WCRCGAL [47] Wheat AI 0.28(26 %) SGPWSWCNPATGYKVSALTGCRAMVKLQ-CV-----GSQV-----PEAVLRDCCQQLADINNEWCRCGDL [48] TPAP-LCQPGMGYPMYPLPRCRALVK-RQC-V----GRGTAAAAEQVR-RD-CCRQLAAVDDSWCRCEAI [57] Rice A14 (33 %) DHHKDQVVYSLGE-RCQPGMGYPMYSLPRCR-AVVKRQC-V-GTR-SPG-AVDEQ-L-AQDCCRELAAVDDSWCRCSAL [58] Barley pUP13 (33 %) ERDYGEYCRVGKSIPINPLPACREYI-TRRCAV----GDQQV----PDVLKQQCCRELSDLPES-CRCDAL [57] Rice AG2 (32 %) [40] Ragi bifunctional inhibitor RILMDGVVTSS--GQHEGRLLQD-LPGCPRQVQRAF-APKLVTEVECNLATIHG-G----PFCLSLLGAGE Members known as trypsin inhibitor [41] Maize TI (66 %) SILMDGAIPPGPDAQLEGR-LED-LPGCPREVQRGF-AATLVTEAECNLATISG-V----AECPWILGGGTMPSK [42] Rye TI (62 %) RILMDGVVTQQ--GVFEGGYLKD-MPNCPRVTQRSY-AATLVAPQECNLPTIHG-S----PYCPTLQAG [43] Barley TI/CMe (56 %) RIIMQGVVTWQ--GAFEGAYFKD-SPNCPRERQTSY-AANLVTPQECNLGTIHG-S----AYCPELQPGYGVVL…”

“…An alignment of the RBI sequence [40] with known sequences of other members of the cereal inhibitor superfamily [41][42][43][44][45][46][47][48][49][50][51][52][53][54][55][56][57][58][59]. The regular secondary structures of RBI in the structure of the RBI-TMA complex are indicated as follows: ===, α helices; ^^^, β strands; xxx, 3 10 helices.…”

Complete amino acid sequence of the α-amylase/subtilisin inhibitor from barley

“…However, more and more evidence has accumulated showing close relationships between various protease and a-amylase inhibitors. Thus, the a-amylase/ trypsin inhibitor from ragi (4) is homologous with trypsin inhibitors isolated from corn (17) and barley (23) and with a-amylase inhibitors isolated from wheat (16,22,24). Similarly, an a-amylase inhibitor isolated from ragi (5) is homologous with a protein from barley having a M.W.…”

The promoter of barley trypsin-inhibitor BTI-CMe, discriminates between wheat and barley endosperm protoplasts in transient expression assays

“…This 13 kDa protein, which is very abundant in barley endosperm, inhibits trypsin but is inactive against other proteases such as chymotrypsin, elastase, papain, pepsin or the endogenous proteases of green malt (Mikola and Soulinna 1969) and does not inhibit a-amylases (Barber et al 1986). As its maize homologue (Mahoney et al 1984), the BTI-CMe is also active towards plasma kallikrein and the activated Hageman factor (6-factor XII a of the blood clotting cascade) (Chong and Reeck 19 87) . Both cDNA and genomic clones have been characterized and BTI-CMe gene expression has been shown to be dependent on trans acting factor(s) (Rodriguez-Palenzuela et al 1989, Royo 1991.…”